A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping (421 views)
Cells (ISSN: 2073-4409linking, 2073-4409electronic), 2020 May 20; 9(5): 1297-1297.
Export to BibTeX Export to EndNote
Paper type: Review, Journal Article
Impact factor: 6.6, 5-year impact factor: 5.276
Url: https://www.mdpi.com/2073-4409/9/5/1267
Keywords: Sars-Cov-2, Covid-19, Rna Replication Machinery, Structural Biology, Coronavirus, Animals, Betacoronavirus Genetics, Catalytic Domain, Coronavirus Infections Virology, Dna-Directed Rna Polymerases Metabolism, Exoribonucleases Chemistry Metabolism, Genome, Viral Genetics, Humans, Methyltransferases Chemistry Metabolism, Pandemics, Pneumonia, Viral Virology, Protein Conformation, Alpha-Helical, Rna Helicases Chemistry Metabolism, Messenger Metabolism, Viral Metabolism, Viral Nonstructural Proteins Chemistry Metabolism, Viral Regulatory And Accessory Proteins Chemistry Metabolism, Virus Replication Physiology, Infectious Disease, Protein Structure
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, IBB, CNR, 80134 Naples
Institute of Molecular Genetics, IGM, CNR, 27100 Pavia
References:
1. Zhou P., Yang X.L., Wang X.G., Hu B., Zhang L., Zhang W., Si H.R., Zhu Y., Li B., Huang C.L., et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020;579:270–273. doi: 10.1038/s41586-020-2012-7. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
2. Wu J.T., Leung K., Leung G.M. Nowcasting and forecasting the potential domestic and international spread of the 2019-nCoV outbreak originating in Wuhan, China: A modelling study. Lancet. 2020;395:689–697. doi: 10.1016/S0140-6736(20)30260-9. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
3. Lu R., Zhao X., Li J., Niu P., Yang B., Wu H., Wang W., Song H., Huang B., Zhu N., et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: Implications for virus origins and receptor binding. Lancet. 2020;395:565–574. doi: 10.1016/S0140-6736(20)30251-8. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
4. Luan J., Lu Y., Jin X., Zhang L. Spike protein recognition of mammalian ACE2 predicts the host range and an optimized ACE2 for SARS-CoV-2 infection. Biochem. Biophys. Res. Commun. 2020 doi: 10.1016/j.bbrc.2020.03.047. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
5. Wrapp D., Wang N., Corbett K.S., Goldsmith J.A., Hsieh C.L., Abiona O., Graham B.S., McLellan J.S. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020;367:1260–1263. doi: 10.1126/science.abb2507. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
6. Wang K., Chen W., Zhou Y.-S., Lian J.-Q., Zhang Z., Du P., Gong L., Zhang Y., Cui H.-Y., Geng J.-J., et al. SARS-CoV-2 invades host cells via a novel route: CD147-spike protein. BioRxiv. 2020 doi: 10.1101/2020.03.14.988345. [CrossRef] [Google Scholar]
7. Hoffmann M., Kleine-Weber H., Schroeder S., Krüger N., Herrler T., Erichsen S., Schiergens T.S., Herrler G., Wu N.H., Nitsche A., et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. 2020 doi: 10.1016/j.cell.2020.02.052. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
8. Yang N., Shen H.M. Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19. Int. J. Biol. Sci. 2020;16:1724–1731. doi: 10.7150/ijbs.45498. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
9. Xia S., Zhu Y., Liu M., Lan Q., Xu W., Wu Y., Ying T., Liu S., Shi Z., Jiang S., et al. Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. Cell. Mol. Immunol. 2020 doi: 10.1038/s41423-020-0374-2. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
10. Gordon D.E., Jang G.M., Bouhaddou M., Krogan N.J. A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing. BioXriv. 2020 doi: 10.1038/s41586-020-2286-9. [PubMed] [CrossRef] [Google Scholar]
11. Brai A., Martelli F., Riva V., Garbelli A., Fazi R., Zamperini C., Pollutri A., Falsitta L., Ronzini S., Maccari L., et al. DDX3X Helicase Inhibitors as a New Strategy To Fight the West Nile Virus Infection. J Med. Chem. 2019;62:2333–2347. doi: 10.1021/acs.jmedchem.8b01403. [PubMed] [CrossRef] [Google Scholar]
12. Brai A., Fazi R., Tintori C., Zamperini C., Bugli F., Sanguinetti M., Stigliano E., Este J., Badia R., Franco S., et al. Human DDX3 protein is a valuable target to develop broad spectrum antiviral agents. Proc. Natl. Acad. Sci. USA. 2016;113:5388–5393. doi: 10.1073/pnas.1522987113. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
13. Wu A., Peng Y., Huang B., Ding X., Wang X., Niu P., Meng J., Zhu Z., Zhang Z., Wang J., et al. Genome Composition and Divergence of the Novel Coronavirus (2019-nCoV) Originating in China. Cell Host Microbe. 2020;27:325–328. doi: 10.1016/j.chom.2020.02.001. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
14. Sola I., Almazan F., Zuniga S., Enjuanes L. Continuous and Discontinuous RNA Synthesis in Coronaviruses. Annu. Rev. Virol. 2015;2:265–288. doi: 10.1146/annurev-virology-100114-055218. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
15. Gorbalenya A.E., Enjuanes L., Ziebuhr J., Snijder E.J. Nidovirales: Evolving the largest RNA virus genome. Virus Res. 2006;117:17–37. doi: 10.1016/j.virusres.2006.01.017. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
16. Wu F., Zhao S., Yu B., Chen Y.M., Wang W., Song Z.G., Hu Y., Tao Z.W., Tian J.H., Pei Y.Y., et al. A new coronavirus associated with human respiratory disease in China. Nature. 2020;579:265–269. doi: 10.1038/s41586-020-2008-3. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
17. Dufour D., Mateos-Gomez P.A., Enjuanes L., Gallego J., Sola I. Structure and functional relevance of a transcription-regulating sequence involved in coronavirus discontinuous RNA synthesis. J. Virol. 2011;85:4963–4973. doi: 10.1128/JVI.02317-10. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
18. Mateos-Gomez P.A., Morales L., Zuniga S., Enjuanes L., Sola I. Long-distance RNA-RNA interactions in the coronavirus genome form high-order structures promoting discontinuous RNA synthesis during transcription. J. Virol. 2013;87:177–186. doi: 10.1128/JVI.01782-12. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
19. Knoops K., Kikkert M., Worm S.H., Zevenhoven-Dobbe J.C., van der Meer Y., Koster A.J., Mommaas A.M., Snijder E.J. SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol. 2008;6:e226. doi: 10.1371/journal.pbio.0060226. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
20. Cheng A., Zhang W., Xie Y., Jiang W., Arnold E., Sarafianos S.G., Ding J. Expression, purification, and characterization of SARS coronavirus RNA polymerase. Virology. 2005;335:165–176. doi: 10.1016/j.virol.2005.02.017. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
21. Ivanov K.A., Thiel V., Dobbe J.C., van der Meer Y., Snijder E.J., Ziebuhr J. Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase. J. Virol. 2004;78:5619–5632. doi: 10.1128/JVI.78.11.5619-5632.2004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
22. Feder M., Pas J., Wyrwicz L.S., Bujnicki J.M. Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2’-O-methyltransferases. Gene. 2003;302:129–138. doi: 10.1016/S0378-1119(02)01097-1. [PubMed] [CrossRef] [Google Scholar]
23. Snijder E.J., Bredenbeek P.J., Dobbe J.C., Thiel V., Ziebuhr J., Poon L.L., Guan Y., Rozanov M., Spaan W.J., Gorbalenya A.E. Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J. Mol. Biol. 2003;331:991–1004. doi: 10.1016/S0022-2836(03)00865-9. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
24. Sevajol M., Subissi L., Decroly E., Canard B., Imbert I. Insights into RNA synthesis, capping, and proofreading mechanisms of SARS-coronavirus. Virus Res. 2014;194:90–99. doi: 10.1016/j.virusres.2014.10.008. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
25. Bhardwaj K., Guarino L., Kao C.C. The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor. J. Virol. 2004;78:12218–12224. doi: 10.1128/JVI.78.22.12218-12224.2004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
26. Ivanov K.A., Hertzig T., Rozanov M., Bayer S., Thiel V., Gorbalenya A.E., Ziebuhr J. Major genetic marker of nidoviruses encodes a replicative endoribonuclease. Proc. Natl. Acad. Sci. USA. 2004;101:12694–12699. doi: 10.1073/pnas.0403127101. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
27. Deng X., Hackbart M., Mettelman R.C., O’Brien A., Mielech A.M., Yi G., Kao C.C., Baker S.C. Coronavirus nonstructural protein 15 mediates evasion of dsRNA sensors and limits apoptosis in macrophages. Proc. Natl. Acad. Sci. USA. 2017;114:E4251–E4260. doi: 10.1073/pnas.1618310114. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
28. Imbert I., Guillemot J.C., Bourhis J.M., Bussetta C., Coutard B., Egloff M.P., Ferron F., Gorbalenya A.E., Canard B. A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus. EMBO J. 2006;25:4933–4942. doi: 10.1038/sj.emboj.7601368. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
29. Subissi L., Posthuma C.C., Collet A., Zevenhoven-Dobbe J.C., Gorbalenya A.E., Decroly E., Snijder E.J., Canard B., Imbert I. One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc. Natl. Acad. Sci. USA. 2014;111:E3900–E3909. doi: 10.1073/pnas.1323705111. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
30. Bouvet M., Lugari A., Posthuma C.C., Zevenhoven J.C., Bernard S., Betzi S., Imbert I., Canard B., Guillemot J.C., Lécine P., et al. Coronavirus Nsp10, a critical co-factor for activation of multiple replicative enzymes. J. Biol. Chem. 2014;289:25783–25796. doi: 10.1074/jbc.M114.577353. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
31. Angelini M.M., Akhlaghpour M., Neuman B.W., Buchmeier M.J. Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles. mBio. 2013;4 doi: 10.1128/mBio.00524-13. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
32. Sawicki S.G., Sawicki D.L., Siddell S.G. A contemporary view of coronavirus transcription. J. Virol. 2007;81:20–29. doi: 10.1128/JVI.01358-06. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
33. Kamitani W., Huang C., Narayanan K., Lokugamage K.G., Makino S. A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein. Nat. Struct. Mol. Biol. 2009;16:1134–1140. doi: 10.1038/nsmb.1680. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
34. Narayanan K., Huang C., Lokugamage K., Kamitani W., Ikegami T., Tseng C.T., Makino S. Severe acute respiratory syndrome coronavirus nsp1 suppresses host gene expression, including that of type I interferon, in infected cells. J. Virol. 2008;82:4471–4479. doi: 10.1128/JVI.02472-07. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
35. McBride R., van Zyl M., Fielding B.C. The coronavirus nucleocapsid is a multifunctional protein. Viruses. 2014;6:2991–3018. doi: 10.3390/v6082991. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
36. De Haan C.A., Rottier P.J. Molecular interactions in the assembly of coronaviruses. Adv. Virus Res. 2005;64:165–230. doi: 10.1016/S0065-3527(05)64006-7. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
37. Lai M.M., Cavanagh D. The molecular biology of coronaviruses. Adv. Virus Res. 1997;48:1–100. [PMC free article] [PubMed] [Google Scholar]
38. Tahara S.M., Dietlin T.A., Bergmann C.C., Nelson G.W., Kyuwa S., Anthony R.P., Stohlman S.A. Coronavirus translational regulation: Leader affects mRNA efficiency. Virology. 1994;202:621–630. doi: 10.1006/viro.1994.1383. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
39. Tahara S.M., Dietlin T.A., Nelson G.W., Stohlman S.A., Manno D.J. Mouse hepatitis virus nucleocapsid protein as a translational effector of viral mRNAs. Adv. Exp. Med. Biol. 1998;440:313–318. doi: 10.1007/978-1-4615-5331-1_41. [PubMed] [CrossRef] [Google Scholar]
40. Chang C.K., Hou M.H., Chang C.F., Hsiao C.D., Huang T.H. The SARS coronavirus nucleocapsid protein--forms and functions. Antivir. Res. 2014;103:39–50. doi: 10.1016/j.antiviral.2013.12.009. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
41. Sturman L.S., Holmes K.V., Behnke J. Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid. J. Virol. 1980;33:449–462. doi: 10.1128/JVI.33.1.449-462.1980. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
42. Kuo L., Masters P.S. Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus. J. Virol. 2002;76:4987–4999. doi: 10.1128/JVI.76.10.4987-4999.2002. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
43. De Haan C.A., Kuo L., Masters P.S., Vennema H., Rottier P.J. Coronavirus particle assembly: Primary structure requirements of the membrane protein. J. Virol. 1998;72:6838–6850. doi: 10.1128/JVI.72.8.6838-6850.1998. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
44. De Haan C.A., Smeets M., Vernooij F., Vennema H., Rottier P.J. Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein. J. Virol. 1999;73:7441–7452. doi: 10.1128/JVI.73.9.7441-7452.1999. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
45. Peti W., Johnson M.A., Herrmann T., Neuman B.W., Buchmeier M.J., Nelson M., Joseph J., Page R., Stevens R.C., Kuhn P., et al. Structural genomics of the severe acute respiratory syndrome coronavirus: Nuclear magnetic resonance structure of the protein nsP7. J. Virol. 2005;79:12905–12913. doi: 10.1128/JVI.79.20.12905-12913.2005. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
46. Johnson M.A., Jaudzems K., Wüthrich K. NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5. J. Mol. Biol. 2010;402:619–628. doi: 10.1016/j.jmb.2010.07.043. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
47. Zhai Y., Sun F., Li X., Pang H., Xu X., Bartlam M., Rao Z. Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer. Nat. Struct. Mol. Biol. 2005;12:980–986. doi: 10.1038/nsmb999. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
48. Kirchdoerfer R.N., Ward A.B. Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. Nat. Commun. 2019;10:2342. doi: 10.1038/s41467-019-10280-3. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
49. Littler D.R., Gully B.S., Colson R.N., Rossjohn J. Crystal structure of the SARS-CoV-2 non-structural protein 9, Nsp9. BioXriv. 2020 doi: 10.1101/2020.03.28.013920. [CrossRef] [Google Scholar]
50. Egloff M.P., Ferron F., Campanacci V., Longhi S., Rancurel C., Dutartre H., Snijder E.J., Gorbalenya A.E., Cambillau C., Canard B. The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world. Proc. Natl. Acad. Sci. USA. 2004;101:3792–3796. doi: 10.1073/pnas.0307877101. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
51. Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J., Berrow N., Owens R., Gilbert R., Davidson A., et al. The nsp9 replicase protein of SARS-coronavirus, structure and functional insights. Structure. 2004;12:341–353. doi: 10.1016/j.str.2004.01.016. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
52. Decroly E., Debarnot C., Ferron F., Bouvet M., Coutard B., Imbert I., Gluais L., Papageorgiou N., Sharff A., Bricogne G., et al. Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2 ‘-O-Methyltransferase nsp10/nsp16 Complex. PLoS Pathog. 2011;7:e1002059. doi: 10.1371/journal.ppat.1002059. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
53. Chen Y., Su C.Y., Ke M., Jin X., Xu L.R., Zhang Z., Wu A.D., Sun Y., Yang Z.N., Tien P., et al. Biochemical and Structural Insights into the Mechanisms of SARS Coronavirus RNA Ribose 2 ‘-O-Methylation by nsp16/nsp10 Protein Complex. PLoS Pathog. 2011;7:e1002294. doi: 10.1371/journal.ppat.1002294. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
54. Ferron F., Subissi L., De Morais A.T.S., Le N.T.T., Sevajol M., Gluais L., Decroly E., Vonrhein C., Bricogne G., Canard B., et al. Structural and molecular basis of mismatch correction and ribavirin excision from coronavirus RNA. Proc. Natl. Acad. Sci. USA. 2018;115:E162–E171. doi: 10.1073/pnas.1718806115. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
55. Ma Y., Wu L., Shaw N., Gao Y., Wang J., Sun Y., Lou Z., Yan L., Zhang R., Rao Z. Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex. Proc. Natl. Acad. Sci. USA. 2015;112:9436–9441. doi: 10.1073/pnas.1508686112. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
56. Su D., Lou Z.Y., Sun F., Zhai Y.J., Yang H.T., Zhang R.G., Joachimiak A., Zhang X.J.C., Bartlam M., Rao Z.H. Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10. J. Virol. 2006;80:7902–7908. doi: 10.1128/JVI.00483-06. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
57. Gao Y., Yan L., Huang Y., Liu F., Zhao Y., Cao L., Wang T., Sun Q., Ming Z., Zhang L., et al. Structure of the RNA-dependent RNA polymerase from COVID-19 virus. Science. 2020 doi: 10.1126/science.abb7498. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
58. Yin W., Mao C., Luan X., Shen D.-D., Shen Q., Su H., Wang X., Zhou F., Zhao W., Gao M., et al. Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir. BioXriv. 2020 doi: 10.1126/science.abc1560. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
59. Jia Z., Yan L., Ren Z., Wu L., Wang J., Guo J., Zheng L., Ming Z., Zhang L., Lou Z., et al. Delicate structural coordination of the Severe Acute Respiratory Syndrome coronavirus Nsp13 upon ATP hydrolysis. Nucleic Acids Res. 2019;47:6538–6550. doi: 10.1093/nar/gkz409. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
60. Hao W., Wojdyla J.A., Zhao R., Han R., Das R., Zlatev I., Manoharan M., Wang M., Cui S. Crystal structure of Middle East respiratory syndrome coronavirus helicase. PLoS Pathog. 2017;13:e1006474. doi: 10.1371/journal.ppat.1006474. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
61. Kim Y., Jedrzejczak R., Maltseva N.I., Wilamowski M., Endres M., Godzik A., Michalska K., Joachimiak A. Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2. BioXriv. 2020 doi: 10.1002/pro.3873. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
62. Ricagno S., Egloff M.P., Ulferts R., Coutard B., Nurizzo D., Campanacci V., Cambillau C., Ziebuhr J., Canard B. Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family. Proc. Natl. Acad. Sci. USA. 2006;103:11892–11897. doi: 10.1073/pnas.0601708103. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
63. Bhardwaj K., Palaninathan S., Alcantara J.M., Yi L.L., Guarino L., Sacchettini J.C., Kao C.C. Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15. J. Biol. Chem. 2008;283:3655–3664. doi: 10.1074/jbc.M708375200. [PubMed] [CrossRef] [Google Scholar]
64. Cameron C.E., Götte M., Raney K.D. Viral Genome Replication. Springer; Boston, MA, USA: 2009. [Google Scholar]
65. Von Brunn A., Teepe C., Simpson J.C., Pepperkok R., Friedel C.C., Zimmer R., Roberts R., Baric R., Haas J. Analysis of intraviral protein-protein interactions of the SARS coronavirus ORFeome. PLoS ONE. 2007;2:e459. doi: 10.1371/journal.pone.0000459. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
66. Tan Y.W., Fung T.S., Shen H., Huang M., Liu D.X. Coronavirus infectious bronchitis virus non-structural proteins 8 and 12 form stable complex independent of the non-translated regions of viral RNA and other viral proteins. Virology. 2018;513:75–84. doi: 10.1016/j.virol.2017.10.004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
67. Seybert A., Posthuma C.C., van Dinten L.C., Snijder E.J., Gorbalenya A.E., Ziebuhr J. A complex zinc finger controls the enzymatic activities of nidovirus helicases. J. Virol. 2005;79:696–704. doi: 10.1128/JVI.79.2.696-704.2005. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
68. Lehmann K.C., Snijder E.J., Posthuma C.C., Gorbalenya A.E. What we know but do not understand about nidovirus helicases. Virus Res. 2015;202:12–32. doi: 10.1016/j.virusres.2014.12.001. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
69. Brockway S.M., Clay C.T., Lu X.T., Denison M.R. Characterization of the expression, intracellular localization, and replication complex association of the putative mouse hepatitis virus RNA-dependent RNA polymerase. J. Virol. 2003;77:10515–10527. doi: 10.1128/JVI.77.19.10515-10527.2003. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
70. Zhang L., Li L., Yan L., Ming Z., Jia Z., Lou Z., Rao Z. Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus. J. Virol. 2018;92:e00893-18. doi: 10.1128/JVI.00893-18. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
71. Athmer J., Fehr A.R., Grunewald M., Smith E.C., Denison M.R., Perlman S. In Situ Tagged nsp15 Reveals Interactions with Coronavirus Replication/Transcription Complex-Associated Proteins. mBio. 2017;8:e02320-16. doi: 10.1128/mBio.02320-16. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
72. Deming D.J., Graham R.L., Denison M.R., Baric R.S. Processing of open reading frame 1a replicase proteins nsp7 to nsp10 in murine hepatitis virus strain A59 replication. J. Virol. 2007;81:10280–10291. doi: 10.1128/JVI.00017-07. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
73. Lehmann K.C., Gulyaeva A., Zevenhoven-Dobbe J.C., Janssen G.M., Ruben M., Overkleeft H.S., van Veelen P.A., Samborskiy D.V., Kravchenko A.A., Leontovich A.M., et al. Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses. Nucleic Acids Res. 2015;43:8416–8434. doi: 10.1093/nar/gkv838. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
74. Liau N.P.D., Laktyushin A., Lucet I.S., Murphy J.M., Yao S., Whitlock E., Callaghan K., Nicola N.A., Kershaw N.J., Babon J.J. The molecular basis of JAK/STAT inhibition by SOCS1. Nat. Commun. 2018;9:1558. doi: 10.1038/s41467-018-04013-1. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
75. Arnold J.J., Cameron C.E. Poliovirus RNA-dependent RNA polymerase (3D(pol)). Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub) J. Biol. Chem. 2000;275:5329–5336. doi: 10.1074/jbc.275.8.5329. [PubMed] [CrossRef] [Google Scholar]
76. Arias A., Arnold J.J., Sierra M., Smidansky E.D., Domingo E., Cameron C.E. Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin. J. Virol. 2008;82:12346–12355. doi: 10.1128/JVI.01297-08. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
77. Gong P., Peersen O.B. Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc. Natl. Acad. Sci. USA. 2010;107:22505–22510. doi: 10.1073/pnas.1007626107. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
78. Warren T.K., Jordan R., Lo M.K., Ray A.S., Mackman R.L., Soloveva V., Siegel D., Perron M., Bannister R., Hui H.C., et al. Therapeutic efficacy of the small molecule GS-5734 against Ebola virus in rhesus monkeys. Nature. 2016;531:381–385. doi: 10.1038/nature17180. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
79. Agostini M.L., Andres E.L., Sims A.C., Graham R.L., Sheahan T.P., Lu X., Smith E.C., Case J.B., Feng J.Y., Jordan R., et al. Coronavirus Susceptibility to the Antiviral Remdesivir (GS-5734) Is Mediated by the Viral Polymerase and the Proofreading Exoribonuclease. mBio. 2018;9:e00221-18. doi: 10.1128/mBio.00221-18. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
80. Brown A.J., Won J.J., Graham R.L., Dinnon K.H., 3rd, Sims A.C., Feng J.Y., Cihlar T., Denison M.R., Baric R.S., Sheahan T.P. Broad spectrum antiviral remdesivir inhibits human endemic and zoonotic deltacoronaviruses with a highly divergent RNA dependent RNA polymerase. Antivir. Res. 2019;169:104541. doi: 10.1016/j.antiviral.2019.104541. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
81. Wang M., Cao R., Zhang L., Yang X., Liu J., Xu M., Shi Z., Hu Z., Zhong W., Xiao G. Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro. Cell Res. 2020;30:269–271. doi: 10.1038/s41422-020-0282-0. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
82. De Wit E., Feldmann F., Cronin J., Jordan R., Okumura A., Thomas T., Scott D., Cihlar T., Feldmann H. Prophylactic and therapeutic remdesivir (GS-5734) treatment in the rhesus macaque model of MERS-CoV infection. Proc. Natl. Acad. Sci. USA. 2020;117:6771–6776. doi: 10.1073/pnas.1922083117. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
83. Lo M.K., Jordan R., Arvey A., Sudhamsu J., Shrivastava-Ranjan P., Hotard A.L., Flint M., McMullan L.K., Siegel D., Clarke M.O., et al. GS-5734 and its parent nucleoside analog inhibit Filo-, Pneumo-, and Paramyxoviruses. Sci Rep. 2017;7:43395. doi: 10.1038/srep43395. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
84. Sheahan T.P., Sims A.C., Graham R.L., Menachery V.D., Gralinski L.E., Case J.B., Leist S.R., Pyrc K., Feng J.Y., Trantcheva I., et al. Broad-spectrum antiviral GS-5734 inhibits both epidemic and zoonotic coronaviruses. Sci. Transl. Med. 2017;9 doi: 10.1126/scitranslmed.aal3653. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
85. Sheahan T.P., Sims A.C., Leist S.R., Schafer A., Won J., Brown A.J., Montgomery S.A., Hogg A., Babusis D., Clarke M.O., et al. Comparative therapeutic efficacy of remdesivir and combination lopinavir, ritonavir, and interferon beta against MERS-CoV. Nat. Commun. 2020;11:222. doi: 10.1038/s41467-019-13940-6. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
86. Cardile A.P., Warren T.K., Martins K.A., Reisler R.B., Bavari S. Will There Be a Cure for Ebola? Annu. Rev. Pharmacol. Toxicol. 2017;57:329–348. doi: 10.1146/annurev-pharmtox-010716-105055. [PubMed] [CrossRef] [Google Scholar]
87. Jordan P.C., Liu C., Raynaud P., Lo M.K., Spiropoulou C.F., Symons J.A., Beigelman L., Deval J. Initiation, extension, and termination of RNA synthesis by a paramyxovirus polymerase. PLoS Pathog. 2018;14:e1006889. doi: 10.1371/journal.ppat.1006889. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
88. Tchesnokov E.P., Feng J.Y., Porter D.P., Gotte M. Mechanism of Inhibition of Ebola Virus RNA-Dependent RNA Polymerase by Remdesivir. Viruses. 2019;11:326. doi: 10.3390/v11040326. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
89. Gordon C.J., Tchesnokov E.P., Feng J.Y., Porter D.P., Gotte M. The antiviral compound remdesivir potently inhibits RNA-dependent RNA polymerase from Middle East respiratory syndrome coronavirus. J. Biol. Chem. 2020;295:4773–4779. doi: 10.1074/jbc.AC120.013056. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
90. Holshue M.L., DeBolt C., Lindquist S., Lofy K.H., Wiesman J., Bruce H., Spitters C., Ericson K., Wilkerson S., Tural A., et al. First Case of 2019 Novel Coronavirus in the United States. N. Engl. J. Med. 2020;382:929–936. doi: 10.1056/NEJMoa2001191. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
91. Lai C.C., Shih T.P., Ko W.C., Tang H.J., Hsueh P.R. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and coronavirus disease-2019 (COVID-19): The epidemic and the challenges. Int. J. Antimicrob. Agents. 2020;55:105924. doi: 10.1016/j.ijantimicag.2020.105924. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
92. Ogando N.S., Ferron F., Decroly E., Canard B., Posthuma C.C., Snijder E.J. The Curious Case of the Nidovirus Exoribonuclease: Its Role in RNA Synthesis and Replication Fidelity. Front. Microbiol. 2019;10:1813. doi: 10.3389/fmicb.2019.01813. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
93. Becares M., Pascual-Iglesias A., Nogales A., Sola I., Enjuanes L., Zuniga S. Mutagenesis of Coronavirus nsp14 Reveals Its Potential Role in Modulation of the Innate Immune Response. J. Virol. 2016;90:5399–5414. doi: 10.1128/JVI.03259-15. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
94. Eckerle L.D., Lu X., Sperry S.M., Choi L., Denison M.R. High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants. J. Virol. 2007;81:12135–12144. doi: 10.1128/JVI.01296-07. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
95. Eckerle L.D., Becker M.M., Halpin R.A., Li K., Venter E., Lu X.T., Scherbakova S., Graham R.L., Baric R.S., Stockwell T.B., et al. Infidelity of SARS-CoV Nsp14-Exonuclease Mutant Virus Replication Is Revealed by Complete Genome Sequencing. PLoS Pathog. 2010;6:e1000896. doi: 10.1371/journal.ppat.1000896. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
96. Marcotrigiano J., Gingras A.C., Sonenberg N., Burley S.K. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell. 1997;89:951–961. doi: 10.1016/S0092-8674(00)80280-9. [PubMed] [CrossRef] [Google Scholar]
97. Decroly E., Ferron F., Lescar J., Canard B. Conventional and unconventional mechanisms for capping viral mRNA. Nat. Rev. Microbiol. 2012;10:51–65. doi: 10.1038/nrmicro2675. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
98. Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E. RNA 3 ‘-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. Proc. Natl. Acad. Sci. USA. 2012;109:9372–9377. doi: 10.1073/pnas.1201130109. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
99. Derbyshire V., Grindley N.D.F., Joyce C.M. The 3′–5′ Exonuclease of DNA-Polymerase-I of Escherichia-Coli—Contribution of Each Amino-Acid at the Active-Site to the Reaction. EMBO J. 1991;10:17–24. doi: 10.1002/j.1460-2075.1991.tb07916.x. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
100. Romano M., Squeglia F., Berisio R. Structure and Function of RNase AS: A Novel Virulence Factor From Mycobacterium tuberculosis. Curr. Med. Chem. 2015;22:1745–1756. doi: 10.2174/0929867322666150417125301. [PubMed] [CrossRef] [Google Scholar]
101. Romano M., van de Weerd R., Brouwer F.C., Roviello G.N., Lacroix R., Sparrius M., van den Brink-van Stempvoort G., Maaskant J.J., van der Sar A.M., Appelmelk B.J., et al. Structure and function of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo. Structure. 2014;22:719–730. doi: 10.1016/j.str.2014.01.014. [PubMed] [CrossRef] [Google Scholar]
102. Minskaia E., Hertzig T., Gorbalenya A.E., Campanacci V., Cambillau C., Canard B., Ziebuhr J. Discovery of an RNA virus 3 ‘->
5 ‘ exoribonuclease that is critically involved in coronavirus RNA synthesis. Proc. Natl. Acad. Sci. USA. 2006;103:5108–5113. doi: 10.1073/pnas.0508200103. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
103. Calvanese L., Squeglia F., Romano M., D’Auria G., Falcigno L., Berisio R. Structural and dynamic studies provide insights into specificity and allosteric regulation of ribonuclease as, a key enzyme in mycobacterial virulence. J. Biomol. Struct. Dyn. 2019:1–13. doi: 10.1080/07391102.2019.1643786. [PubMed] [CrossRef] [Google Scholar]
104. Denison M.R., Graham R.L., Donaldson E.F., Eckerle L.D., Baric R.S. Coronaviruses an RNA proofreading machine regulates replication fidelity and diversity. RNA Biol. 2011;8:270–279. doi: 10.4161/rna.8.2.15013. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
105. Tchesnokov E.P., Obikhod A., Schinazi R.F., Gotte M. Delayed chain termination protects the anti-hepatitis B virus drug entecavir from excision by HIV-1 reverse transcriptase. J. Biol. Chem. 2008;283:34218–34228. doi: 10.1074/jbc.M806797200. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
106. Dulin D., Arnold J.J., van Laar T., Oh H.S., Lee C., Perkins A.L., Harki D.A., Depken M., Cameron C.E., Dekker N.H. Signatures of Nucleotide Analog Incorporation by an RNA-Dependent RNA Polymerase Revealed Using High-Throughput Magnetic Tweezers. Cell Rep. 2017;21:1063–1076. doi: 10.1016/j.celrep.2017.10.005. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
107. Smith E.C., Blanc H., Surdel M.C., Vignuzzi M., Denison M.R. Coronaviruses lacking exoribonuclease activity are susceptible to lethal mutagenesis: Evidence for proofreading and potential therapeutics. PLoS Pathog. 2013;9:e1003565. doi: 10.1371/journal.ppat.1003565. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
108. Morse J.S., Lalonde T., Xu S., Liu W.R. Learning from the Past: Possible Urgent Prevention and Treatment Options for Severe Acute Respiratory Infections Caused by 2019-nCoV. Chembiochem. 2020;21:730–738. doi: 10.1002/cbic.202000047. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
109. Rao S.T., Rossmann M.G. Comparison of super-secondary structures in proteins. J. Mol. Biol. 1973;76:241–256. doi: 10.1016/0022-2836(73)90388-4. [PubMed] [CrossRef] [Google Scholar]
110. Byszewska M., Smietanski M., Purta E., Bujnicki J.M. RNA methyltransferases involved in 5′ cap biosynthesis. RNA Biol. 2014;11:1597–1607. doi: 10.1080/15476286.2015.1004955. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
111. Chouhan B.P.S., Maimaiti S., Gade M., Laurino P. Rossmann-Fold Methyltransferases: Taking a “beta-Turn” around Their Cofactor, S-Adenosylmethionine. Biochemistry. 2019;58:166–170. doi: 10.1021/acs.biochem.8b00994. [PubMed] [CrossRef] [Google Scholar]
112. Schubert H.L., Blumenthal R.M., Cheng X.D. Many paths to methyltransfer: A chronicle of convergence. Trends Biochem. Sci. 2003;28:329–335. doi: 10.1016/S0968-0004(03)00090-2. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
113. Chen Y., Cai H., Pan J., Xiang N., Tien P., Ahola T., Guo D.Y. Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase. Proc. Natl. Acad. Sci. USA. 2009;106:3484–3489. doi: 10.1073/pnas.0808790106. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
114. Chen Y., Tao J.L., Sun Y., Wu A.D., Su C.Y., Gao G.Z., Cai H., Qiu S., Wu Y.L., Ahola T., et al. Structure-Function Analysis of Severe Acute Respiratory Syndrome Coronavirus RNA Cap Guanine-N7-Methyltransferase. J. Virol. 2013;87:6296–6305. doi: 10.1128/JVI.00061-13. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
115. Jin X., Chen Y., Sun Y., Zeng C., Wang Y., Tao J.L., Wu A.D., Yu X., Zhang Z., Tian J., et al. Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP. Virus Res. 2013;176:45–52. doi: 10.1016/j.virusres.2013.05.001. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
116. Jankowsky E., Fairman M.E. RNA helicases-one fold for many functions. Curr. Opin. Struct. Biol. 2007;17:316–324. doi: 10.1016/j.sbi.2007.05.007. [PubMed] [CrossRef] [Google Scholar]
117. Deng Z., Lehmann K.C., Li X., Feng C., Wang G., Zhang Q., Qi X., Yu L., Zhang X., Feng W., et al. Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase. Nucleic Acids Res. 2014;42:3464–3477. doi: 10.1093/nar/gkt1310. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
118. Ivanov K.A., Ziebuhr J. Human coronavirus 229E nonstructural protein 13: Characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5′-triphosphatase activities. J. Virol. 2004;78:7833–7838. doi: 10.1128/JVI.78.14.7833-7838.2004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
119. Adedeji A.O., Lazarus H. Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase. mSphere. 2016;1:e00235-16. doi: 10.1128/mSphere.00235-16. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
120. Adedeji A.O., Marchand B., Te Velthuis A.J., Snijder E.J., Weiss S., Eoff R.L., Singh K., Sarafianos S.G. Mechanism of nucleic acid unwinding by SARS-CoV helicase. PLoS ONE. 2012;7:e36521. doi: 10.1371/journal.pone.0036521. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
121. Ziebuhr J. The coronavirus replicase. Curr. Top Microbiol. Immunol. 2005;287:57–94. doi: 10.1007/3-540-26765-4_3. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
122. Van Dinten L.C., van Tol H., Gorbalenya A.E., Snijder E.J. The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis. J. Virol. 2000;74:5213–5223. doi: 10.1128/JVI.74.11.5213-5223.2000. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
123. Adedeji A.O., Singh K., Calcaterra N.E., DeDiego M.L., Enjuanes L., Weiss S., Sarafianos S.G. Severe acute respiratory syndrome coronavirus replication inhibitor that interferes with the nucleic acid unwinding of the viral helicase. Antimicrob. Agents Chemother. 2012;56:4718–4728. doi: 10.1128/AAC.00957-12. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
124. Adedeji A.O., Singh K., Kassim A., Coleman C.M., Elliott R., Weiss S.R., Frieman M.B., Sarafianos S.G. Evaluation of SSYA10-001 as a replication inhibitor of severe acute respiratory syndrome, mouse hepatitis, and Middle East respiratory syndrome coronaviruses. Antimicrob. Agents Chemother. 2014;58:4894–4898. doi: 10.1128/AAC.02994-14. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
125. Aouadi W., Blanjoie A., Vasseur J.J., Debart F., Canard B., Decroly E. Binding of the Methyl Donor S-Adenosyl-L-Methionine to Middle East Respiratory Syndrome Coronavirus 2 ‘-O-Methyltransferase nsp16 Promotes Recruitment of the Allosteric Activator nsp10. J. Virol. 2017;91:e02217-16. doi: 10.1128/JVI.02217-16. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
126. Martin J.L., McMillan F.M. SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold. Curr. Opin. Struc. Biol. 2002;12:783–793. doi: 10.1016/S0959-440X(02)00391-3. [PubMed] [CrossRef] [Google Scholar]
127. Joseph J.S., Saikatendu K.S., Subramanian V., Neuman B.W., Brooun A., Griffith M., Moy K., Yadav M.K., Velasquez J., Buchmeier M.J., et al. Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs. J. Virol. 2006;80:7894–7901. doi: 10.1128/JVI.00467-06. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
128. Matthes N., Mesters J.R., Coutard B., Canard B., Snijder E.J., Moll R., Hilgenfeld R. The non-structural protein Nsp10 of mouse hepatitis virus binds zinc ions and nucleic acids. FEBS Lett. 2006;580:4143–4149. doi: 10.1016/j.febslet.2006.06.061. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
129. Zust R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., Szretter K.J., Baker S.C., Barchet W., Diamond M.S., et al. Ribose 2’-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat. Immunol. 2011;12:137–143. doi: 10.1038/ni.1979. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
130. Devarkar S.C., Wang C., Miller M.T., Ramanathan A., Jiang F., Khan A.G., Patel S.S., Marcotrigiano J. Structural basis for m7G recognition and 2’-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I. Proc. Natl. Acad. Sci. USA. 2016;113:596–601. doi: 10.1073/pnas.1515152113. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
131. Hyde J.L., Diamond M.S. Innate immune restriction and antagonism of viral RNA lacking 2-O methylation. Virology. 2015;479–480:66–74. doi: 10.1016/j.virol.2015.01.019. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
132. Daffis S., Szretter K.J., Schriewer J., Li J., Youn S., Errett J., Lin T.Y., Schneller S., Zust R., Dong H., et al. 2’-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature. 2010;468:452–456. doi: 10.1038/nature09489. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
133. Diamond M.S., Farzan M. The broad-spectrum antiviral functions of IFIT and IFITM proteins. Nat. Rev. Immunol. 2013;13:46–57. doi: 10.1038/nri3344. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
1. Zhou P., Yang X.L., Wang X.G., Hu B., Zhang L., Zhang W., Si H.R., Zhu Y., Li B., Huang C.L., et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020;579:270–273. doi: 10.1038/s41586-020-2012-7. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
Cells (ISSN: 2073-4409linking, 2073-4409electronic), 2020 May 20; 9(5): 1297-1297.
Export to BibTeX Export to EndNote
Paper type: Review, Journal Article
Impact factor: 6.6, 5-year impact factor: 5.276
Url: https://www.mdpi.com/2073-4409/9/5/1267
Keywords: Sars-Cov-2, Covid-19, Rna Replication Machinery, Structural Biology, Coronavirus, Animals, Betacoronavirus Genetics, Catalytic Domain, Coronavirus Infections Virology, Dna-Directed Rna Polymerases Metabolism, Exoribonucleases Chemistry Metabolism, Genome, Viral Genetics, Humans, Methyltransferases Chemistry Metabolism, Pandemics, Pneumonia, Viral Virology, Protein Conformation, Alpha-Helical, Rna Helicases Chemistry Metabolism, Messenger Metabolism, Viral Metabolism, Viral Nonstructural Proteins Chemistry Metabolism, Viral Regulatory And Accessory Proteins Chemistry Metabolism, Virus Replication Physiology, Infectious Disease, Protein Structure
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, IBB, CNR, 80134 Naples
Institute of Molecular Genetics, IGM, CNR, 27100 Pavia
References:
1. Zhou P., Yang X.L., Wang X.G., Hu B., Zhang L., Zhang W., Si H.R., Zhu Y., Li B., Huang C.L., et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020;579:270–273. doi: 10.1038/s41586-020-2012-7. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
2. Wu J.T., Leung K., Leung G.M. Nowcasting and forecasting the potential domestic and international spread of the 2019-nCoV outbreak originating in Wuhan, China: A modelling study. Lancet. 2020;395:689–697. doi: 10.1016/S0140-6736(20)30260-9. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
3. Lu R., Zhao X., Li J., Niu P., Yang B., Wu H., Wang W., Song H., Huang B., Zhu N., et al. Genomic characterisation and epidemiology of 2019 novel coronavirus: Implications for virus origins and receptor binding. Lancet. 2020;395:565–574. doi: 10.1016/S0140-6736(20)30251-8. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
4. Luan J., Lu Y., Jin X., Zhang L. Spike protein recognition of mammalian ACE2 predicts the host range and an optimized ACE2 for SARS-CoV-2 infection. Biochem. Biophys. Res. Commun. 2020 doi: 10.1016/j.bbrc.2020.03.047. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
5. Wrapp D., Wang N., Corbett K.S., Goldsmith J.A., Hsieh C.L., Abiona O., Graham B.S., McLellan J.S. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020;367:1260–1263. doi: 10.1126/science.abb2507. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
6. Wang K., Chen W., Zhou Y.-S., Lian J.-Q., Zhang Z., Du P., Gong L., Zhang Y., Cui H.-Y., Geng J.-J., et al. SARS-CoV-2 invades host cells via a novel route: CD147-spike protein. BioRxiv. 2020 doi: 10.1101/2020.03.14.988345. [CrossRef] [Google Scholar]
7. Hoffmann M., Kleine-Weber H., Schroeder S., Krüger N., Herrler T., Erichsen S., Schiergens T.S., Herrler G., Wu N.H., Nitsche A., et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. 2020 doi: 10.1016/j.cell.2020.02.052. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
8. Yang N., Shen H.M. Targeting the Endocytic Pathway and Autophagy Process as a Novel Therapeutic Strategy in COVID-19. Int. J. Biol. Sci. 2020;16:1724–1731. doi: 10.7150/ijbs.45498. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
9. Xia S., Zhu Y., Liu M., Lan Q., Xu W., Wu Y., Ying T., Liu S., Shi Z., Jiang S., et al. Fusion mechanism of 2019-nCoV and fusion inhibitors targeting HR1 domain in spike protein. Cell. Mol. Immunol. 2020 doi: 10.1038/s41423-020-0374-2. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
10. Gordon D.E., Jang G.M., Bouhaddou M., Krogan N.J. A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing. BioXriv. 2020 doi: 10.1038/s41586-020-2286-9. [PubMed] [CrossRef] [Google Scholar]
11. Brai A., Martelli F., Riva V., Garbelli A., Fazi R., Zamperini C., Pollutri A., Falsitta L., Ronzini S., Maccari L., et al. DDX3X Helicase Inhibitors as a New Strategy To Fight the West Nile Virus Infection. J Med. Chem. 2019;62:2333–2347. doi: 10.1021/acs.jmedchem.8b01403. [PubMed] [CrossRef] [Google Scholar]
12. Brai A., Fazi R., Tintori C., Zamperini C., Bugli F., Sanguinetti M., Stigliano E., Este J., Badia R., Franco S., et al. Human DDX3 protein is a valuable target to develop broad spectrum antiviral agents. Proc. Natl. Acad. Sci. USA. 2016;113:5388–5393. doi: 10.1073/pnas.1522987113. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
13. Wu A., Peng Y., Huang B., Ding X., Wang X., Niu P., Meng J., Zhu Z., Zhang Z., Wang J., et al. Genome Composition and Divergence of the Novel Coronavirus (2019-nCoV) Originating in China. Cell Host Microbe. 2020;27:325–328. doi: 10.1016/j.chom.2020.02.001. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
14. Sola I., Almazan F., Zuniga S., Enjuanes L. Continuous and Discontinuous RNA Synthesis in Coronaviruses. Annu. Rev. Virol. 2015;2:265–288. doi: 10.1146/annurev-virology-100114-055218. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
15. Gorbalenya A.E., Enjuanes L., Ziebuhr J., Snijder E.J. Nidovirales: Evolving the largest RNA virus genome. Virus Res. 2006;117:17–37. doi: 10.1016/j.virusres.2006.01.017. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
16. Wu F., Zhao S., Yu B., Chen Y.M., Wang W., Song Z.G., Hu Y., Tao Z.W., Tian J.H., Pei Y.Y., et al. A new coronavirus associated with human respiratory disease in China. Nature. 2020;579:265–269. doi: 10.1038/s41586-020-2008-3. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
17. Dufour D., Mateos-Gomez P.A., Enjuanes L., Gallego J., Sola I. Structure and functional relevance of a transcription-regulating sequence involved in coronavirus discontinuous RNA synthesis. J. Virol. 2011;85:4963–4973. doi: 10.1128/JVI.02317-10. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
18. Mateos-Gomez P.A., Morales L., Zuniga S., Enjuanes L., Sola I. Long-distance RNA-RNA interactions in the coronavirus genome form high-order structures promoting discontinuous RNA synthesis during transcription. J. Virol. 2013;87:177–186. doi: 10.1128/JVI.01782-12. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
19. Knoops K., Kikkert M., Worm S.H., Zevenhoven-Dobbe J.C., van der Meer Y., Koster A.J., Mommaas A.M., Snijder E.J. SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol. 2008;6:e226. doi: 10.1371/journal.pbio.0060226. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
20. Cheng A., Zhang W., Xie Y., Jiang W., Arnold E., Sarafianos S.G., Ding J. Expression, purification, and characterization of SARS coronavirus RNA polymerase. Virology. 2005;335:165–176. doi: 10.1016/j.virol.2005.02.017. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
21. Ivanov K.A., Thiel V., Dobbe J.C., van der Meer Y., Snijder E.J., Ziebuhr J. Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase. J. Virol. 2004;78:5619–5632. doi: 10.1128/JVI.78.11.5619-5632.2004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
22. Feder M., Pas J., Wyrwicz L.S., Bujnicki J.M. Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2’-O-methyltransferases. Gene. 2003;302:129–138. doi: 10.1016/S0378-1119(02)01097-1. [PubMed] [CrossRef] [Google Scholar]
23. Snijder E.J., Bredenbeek P.J., Dobbe J.C., Thiel V., Ziebuhr J., Poon L.L., Guan Y., Rozanov M., Spaan W.J., Gorbalenya A.E. Unique and conserved features of genome and proteome of SARS-coronavirus, an early split-off from the coronavirus group 2 lineage. J. Mol. Biol. 2003;331:991–1004. doi: 10.1016/S0022-2836(03)00865-9. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
24. Sevajol M., Subissi L., Decroly E., Canard B., Imbert I. Insights into RNA synthesis, capping, and proofreading mechanisms of SARS-coronavirus. Virus Res. 2014;194:90–99. doi: 10.1016/j.virusres.2014.10.008. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
25. Bhardwaj K., Guarino L., Kao C.C. The severe acute respiratory syndrome coronavirus Nsp15 protein is an endoribonuclease that prefers manganese as a cofactor. J. Virol. 2004;78:12218–12224. doi: 10.1128/JVI.78.22.12218-12224.2004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
26. Ivanov K.A., Hertzig T., Rozanov M., Bayer S., Thiel V., Gorbalenya A.E., Ziebuhr J. Major genetic marker of nidoviruses encodes a replicative endoribonuclease. Proc. Natl. Acad. Sci. USA. 2004;101:12694–12699. doi: 10.1073/pnas.0403127101. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
27. Deng X., Hackbart M., Mettelman R.C., O’Brien A., Mielech A.M., Yi G., Kao C.C., Baker S.C. Coronavirus nonstructural protein 15 mediates evasion of dsRNA sensors and limits apoptosis in macrophages. Proc. Natl. Acad. Sci. USA. 2017;114:E4251–E4260. doi: 10.1073/pnas.1618310114. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
28. Imbert I., Guillemot J.C., Bourhis J.M., Bussetta C., Coutard B., Egloff M.P., Ferron F., Gorbalenya A.E., Canard B. A second, non-canonical RNA-dependent RNA polymerase in SARS coronavirus. EMBO J. 2006;25:4933–4942. doi: 10.1038/sj.emboj.7601368. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
29. Subissi L., Posthuma C.C., Collet A., Zevenhoven-Dobbe J.C., Gorbalenya A.E., Decroly E., Snijder E.J., Canard B., Imbert I. One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc. Natl. Acad. Sci. USA. 2014;111:E3900–E3909. doi: 10.1073/pnas.1323705111. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
30. Bouvet M., Lugari A., Posthuma C.C., Zevenhoven J.C., Bernard S., Betzi S., Imbert I., Canard B., Guillemot J.C., Lécine P., et al. Coronavirus Nsp10, a critical co-factor for activation of multiple replicative enzymes. J. Biol. Chem. 2014;289:25783–25796. doi: 10.1074/jbc.M114.577353. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
31. Angelini M.M., Akhlaghpour M., Neuman B.W., Buchmeier M.J. Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles. mBio. 2013;4 doi: 10.1128/mBio.00524-13. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
32. Sawicki S.G., Sawicki D.L., Siddell S.G. A contemporary view of coronavirus transcription. J. Virol. 2007;81:20–29. doi: 10.1128/JVI.01358-06. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
33. Kamitani W., Huang C., Narayanan K., Lokugamage K.G., Makino S. A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein. Nat. Struct. Mol. Biol. 2009;16:1134–1140. doi: 10.1038/nsmb.1680. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
34. Narayanan K., Huang C., Lokugamage K., Kamitani W., Ikegami T., Tseng C.T., Makino S. Severe acute respiratory syndrome coronavirus nsp1 suppresses host gene expression, including that of type I interferon, in infected cells. J. Virol. 2008;82:4471–4479. doi: 10.1128/JVI.02472-07. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
35. McBride R., van Zyl M., Fielding B.C. The coronavirus nucleocapsid is a multifunctional protein. Viruses. 2014;6:2991–3018. doi: 10.3390/v6082991. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
36. De Haan C.A., Rottier P.J. Molecular interactions in the assembly of coronaviruses. Adv. Virus Res. 2005;64:165–230. doi: 10.1016/S0065-3527(05)64006-7. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
37. Lai M.M., Cavanagh D. The molecular biology of coronaviruses. Adv. Virus Res. 1997;48:1–100. [PMC free article] [PubMed] [Google Scholar]
38. Tahara S.M., Dietlin T.A., Bergmann C.C., Nelson G.W., Kyuwa S., Anthony R.P., Stohlman S.A. Coronavirus translational regulation: Leader affects mRNA efficiency. Virology. 1994;202:621–630. doi: 10.1006/viro.1994.1383. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
39. Tahara S.M., Dietlin T.A., Nelson G.W., Stohlman S.A., Manno D.J. Mouse hepatitis virus nucleocapsid protein as a translational effector of viral mRNAs. Adv. Exp. Med. Biol. 1998;440:313–318. doi: 10.1007/978-1-4615-5331-1_41. [PubMed] [CrossRef] [Google Scholar]
40. Chang C.K., Hou M.H., Chang C.F., Hsiao C.D., Huang T.H. The SARS coronavirus nucleocapsid protein--forms and functions. Antivir. Res. 2014;103:39–50. doi: 10.1016/j.antiviral.2013.12.009. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
41. Sturman L.S., Holmes K.V., Behnke J. Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid. J. Virol. 1980;33:449–462. doi: 10.1128/JVI.33.1.449-462.1980. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
42. Kuo L., Masters P.S. Genetic evidence for a structural interaction between the carboxy termini of the membrane and nucleocapsid proteins of mouse hepatitis virus. J. Virol. 2002;76:4987–4999. doi: 10.1128/JVI.76.10.4987-4999.2002. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
43. De Haan C.A., Kuo L., Masters P.S., Vennema H., Rottier P.J. Coronavirus particle assembly: Primary structure requirements of the membrane protein. J. Virol. 1998;72:6838–6850. doi: 10.1128/JVI.72.8.6838-6850.1998. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
44. De Haan C.A., Smeets M., Vernooij F., Vennema H., Rottier P.J. Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein. J. Virol. 1999;73:7441–7452. doi: 10.1128/JVI.73.9.7441-7452.1999. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
45. Peti W., Johnson M.A., Herrmann T., Neuman B.W., Buchmeier M.J., Nelson M., Joseph J., Page R., Stevens R.C., Kuhn P., et al. Structural genomics of the severe acute respiratory syndrome coronavirus: Nuclear magnetic resonance structure of the protein nsP7. J. Virol. 2005;79:12905–12913. doi: 10.1128/JVI.79.20.12905-12913.2005. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
46. Johnson M.A., Jaudzems K., Wüthrich K. NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5. J. Mol. Biol. 2010;402:619–628. doi: 10.1016/j.jmb.2010.07.043. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
47. Zhai Y., Sun F., Li X., Pang H., Xu X., Bartlam M., Rao Z. Insights into SARS-CoV transcription and replication from the structure of the nsp7-nsp8 hexadecamer. Nat. Struct. Mol. Biol. 2005;12:980–986. doi: 10.1038/nsmb999. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
48. Kirchdoerfer R.N., Ward A.B. Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. Nat. Commun. 2019;10:2342. doi: 10.1038/s41467-019-10280-3. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
49. Littler D.R., Gully B.S., Colson R.N., Rossjohn J. Crystal structure of the SARS-CoV-2 non-structural protein 9, Nsp9. BioXriv. 2020 doi: 10.1101/2020.03.28.013920. [CrossRef] [Google Scholar]
50. Egloff M.P., Ferron F., Campanacci V., Longhi S., Rancurel C., Dutartre H., Snijder E.J., Gorbalenya A.E., Cambillau C., Canard B. The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world. Proc. Natl. Acad. Sci. USA. 2004;101:3792–3796. doi: 10.1073/pnas.0307877101. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
51. Sutton G., Fry E., Carter L., Sainsbury S., Walter T., Nettleship J., Berrow N., Owens R., Gilbert R., Davidson A., et al. The nsp9 replicase protein of SARS-coronavirus, structure and functional insights. Structure. 2004;12:341–353. doi: 10.1016/j.str.2004.01.016. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
52. Decroly E., Debarnot C., Ferron F., Bouvet M., Coutard B., Imbert I., Gluais L., Papageorgiou N., Sharff A., Bricogne G., et al. Crystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2 ‘-O-Methyltransferase nsp10/nsp16 Complex. PLoS Pathog. 2011;7:e1002059. doi: 10.1371/journal.ppat.1002059. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
53. Chen Y., Su C.Y., Ke M., Jin X., Xu L.R., Zhang Z., Wu A.D., Sun Y., Yang Z.N., Tien P., et al. Biochemical and Structural Insights into the Mechanisms of SARS Coronavirus RNA Ribose 2 ‘-O-Methylation by nsp16/nsp10 Protein Complex. PLoS Pathog. 2011;7:e1002294. doi: 10.1371/journal.ppat.1002294. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
54. Ferron F., Subissi L., De Morais A.T.S., Le N.T.T., Sevajol M., Gluais L., Decroly E., Vonrhein C., Bricogne G., Canard B., et al. Structural and molecular basis of mismatch correction and ribavirin excision from coronavirus RNA. Proc. Natl. Acad. Sci. USA. 2018;115:E162–E171. doi: 10.1073/pnas.1718806115. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
55. Ma Y., Wu L., Shaw N., Gao Y., Wang J., Sun Y., Lou Z., Yan L., Zhang R., Rao Z. Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex. Proc. Natl. Acad. Sci. USA. 2015;112:9436–9441. doi: 10.1073/pnas.1508686112. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
56. Su D., Lou Z.Y., Sun F., Zhai Y.J., Yang H.T., Zhang R.G., Joachimiak A., Zhang X.J.C., Bartlam M., Rao Z.H. Dodecamer structure of severe acute respiratory syndrome coronavirus nonstructural protein nsp10. J. Virol. 2006;80:7902–7908. doi: 10.1128/JVI.00483-06. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
57. Gao Y., Yan L., Huang Y., Liu F., Zhao Y., Cao L., Wang T., Sun Q., Ming Z., Zhang L., et al. Structure of the RNA-dependent RNA polymerase from COVID-19 virus. Science. 2020 doi: 10.1126/science.abb7498. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
58. Yin W., Mao C., Luan X., Shen D.-D., Shen Q., Su H., Wang X., Zhou F., Zhao W., Gao M., et al. Structural Basis for the Inhibition of the RNA-Dependent RNA Polymerase from SARS-CoV-2 by Remdesivir. BioXriv. 2020 doi: 10.1126/science.abc1560. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
59. Jia Z., Yan L., Ren Z., Wu L., Wang J., Guo J., Zheng L., Ming Z., Zhang L., Lou Z., et al. Delicate structural coordination of the Severe Acute Respiratory Syndrome coronavirus Nsp13 upon ATP hydrolysis. Nucleic Acids Res. 2019;47:6538–6550. doi: 10.1093/nar/gkz409. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
60. Hao W., Wojdyla J.A., Zhao R., Han R., Das R., Zlatev I., Manoharan M., Wang M., Cui S. Crystal structure of Middle East respiratory syndrome coronavirus helicase. PLoS Pathog. 2017;13:e1006474. doi: 10.1371/journal.ppat.1006474. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
61. Kim Y., Jedrzejczak R., Maltseva N.I., Wilamowski M., Endres M., Godzik A., Michalska K., Joachimiak A. Crystal structure of Nsp15 endoribonuclease NendoU from SARS-CoV-2. BioXriv. 2020 doi: 10.1002/pro.3873. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
62. Ricagno S., Egloff M.P., Ulferts R., Coutard B., Nurizzo D., Campanacci V., Cambillau C., Ziebuhr J., Canard B. Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family. Proc. Natl. Acad. Sci. USA. 2006;103:11892–11897. doi: 10.1073/pnas.0601708103. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
63. Bhardwaj K., Palaninathan S., Alcantara J.M., Yi L.L., Guarino L., Sacchettini J.C., Kao C.C. Structural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15. J. Biol. Chem. 2008;283:3655–3664. doi: 10.1074/jbc.M708375200. [PubMed] [CrossRef] [Google Scholar]
64. Cameron C.E., Götte M., Raney K.D. Viral Genome Replication. Springer; Boston, MA, USA: 2009. [Google Scholar]
65. Von Brunn A., Teepe C., Simpson J.C., Pepperkok R., Friedel C.C., Zimmer R., Roberts R., Baric R., Haas J. Analysis of intraviral protein-protein interactions of the SARS coronavirus ORFeome. PLoS ONE. 2007;2:e459. doi: 10.1371/journal.pone.0000459. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
66. Tan Y.W., Fung T.S., Shen H., Huang M., Liu D.X. Coronavirus infectious bronchitis virus non-structural proteins 8 and 12 form stable complex independent of the non-translated regions of viral RNA and other viral proteins. Virology. 2018;513:75–84. doi: 10.1016/j.virol.2017.10.004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
67. Seybert A., Posthuma C.C., van Dinten L.C., Snijder E.J., Gorbalenya A.E., Ziebuhr J. A complex zinc finger controls the enzymatic activities of nidovirus helicases. J. Virol. 2005;79:696–704. doi: 10.1128/JVI.79.2.696-704.2005. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
68. Lehmann K.C., Snijder E.J., Posthuma C.C., Gorbalenya A.E. What we know but do not understand about nidovirus helicases. Virus Res. 2015;202:12–32. doi: 10.1016/j.virusres.2014.12.001. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
69. Brockway S.M., Clay C.T., Lu X.T., Denison M.R. Characterization of the expression, intracellular localization, and replication complex association of the putative mouse hepatitis virus RNA-dependent RNA polymerase. J. Virol. 2003;77:10515–10527. doi: 10.1128/JVI.77.19.10515-10527.2003. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
70. Zhang L., Li L., Yan L., Ming Z., Jia Z., Lou Z., Rao Z. Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus. J. Virol. 2018;92:e00893-18. doi: 10.1128/JVI.00893-18. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
71. Athmer J., Fehr A.R., Grunewald M., Smith E.C., Denison M.R., Perlman S. In Situ Tagged nsp15 Reveals Interactions with Coronavirus Replication/Transcription Complex-Associated Proteins. mBio. 2017;8:e02320-16. doi: 10.1128/mBio.02320-16. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
72. Deming D.J., Graham R.L., Denison M.R., Baric R.S. Processing of open reading frame 1a replicase proteins nsp7 to nsp10 in murine hepatitis virus strain A59 replication. J. Virol. 2007;81:10280–10291. doi: 10.1128/JVI.00017-07. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
73. Lehmann K.C., Gulyaeva A., Zevenhoven-Dobbe J.C., Janssen G.M., Ruben M., Overkleeft H.S., van Veelen P.A., Samborskiy D.V., Kravchenko A.A., Leontovich A.M., et al. Discovery of an essential nucleotidylating activity associated with a newly delineated conserved domain in the RNA polymerase-containing protein of all nidoviruses. Nucleic Acids Res. 2015;43:8416–8434. doi: 10.1093/nar/gkv838. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
74. Liau N.P.D., Laktyushin A., Lucet I.S., Murphy J.M., Yao S., Whitlock E., Callaghan K., Nicola N.A., Kershaw N.J., Babon J.J. The molecular basis of JAK/STAT inhibition by SOCS1. Nat. Commun. 2018;9:1558. doi: 10.1038/s41467-018-04013-1. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
75. Arnold J.J., Cameron C.E. Poliovirus RNA-dependent RNA polymerase (3D(pol)). Assembly of stable, elongation-competent complexes by using a symmetrical primer-template substrate (sym/sub) J. Biol. Chem. 2000;275:5329–5336. doi: 10.1074/jbc.275.8.5329. [PubMed] [CrossRef] [Google Scholar]
76. Arias A., Arnold J.J., Sierra M., Smidansky E.D., Domingo E., Cameron C.E. Determinants of RNA-dependent RNA polymerase (in)fidelity revealed by kinetic analysis of the polymerase encoded by a foot-and-mouth disease virus mutant with reduced sensitivity to ribavirin. J. Virol. 2008;82:12346–12355. doi: 10.1128/JVI.01297-08. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
77. Gong P., Peersen O.B. Structural basis for active site closure by the poliovirus RNA-dependent RNA polymerase. Proc. Natl. Acad. Sci. USA. 2010;107:22505–22510. doi: 10.1073/pnas.1007626107. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
78. Warren T.K., Jordan R., Lo M.K., Ray A.S., Mackman R.L., Soloveva V., Siegel D., Perron M., Bannister R., Hui H.C., et al. Therapeutic efficacy of the small molecule GS-5734 against Ebola virus in rhesus monkeys. Nature. 2016;531:381–385. doi: 10.1038/nature17180. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
79. Agostini M.L., Andres E.L., Sims A.C., Graham R.L., Sheahan T.P., Lu X., Smith E.C., Case J.B., Feng J.Y., Jordan R., et al. Coronavirus Susceptibility to the Antiviral Remdesivir (GS-5734) Is Mediated by the Viral Polymerase and the Proofreading Exoribonuclease. mBio. 2018;9:e00221-18. doi: 10.1128/mBio.00221-18. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
80. Brown A.J., Won J.J., Graham R.L., Dinnon K.H., 3rd, Sims A.C., Feng J.Y., Cihlar T., Denison M.R., Baric R.S., Sheahan T.P. Broad spectrum antiviral remdesivir inhibits human endemic and zoonotic deltacoronaviruses with a highly divergent RNA dependent RNA polymerase. Antivir. Res. 2019;169:104541. doi: 10.1016/j.antiviral.2019.104541. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
81. Wang M., Cao R., Zhang L., Yang X., Liu J., Xu M., Shi Z., Hu Z., Zhong W., Xiao G. Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro. Cell Res. 2020;30:269–271. doi: 10.1038/s41422-020-0282-0. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
82. De Wit E., Feldmann F., Cronin J., Jordan R., Okumura A., Thomas T., Scott D., Cihlar T., Feldmann H. Prophylactic and therapeutic remdesivir (GS-5734) treatment in the rhesus macaque model of MERS-CoV infection. Proc. Natl. Acad. Sci. USA. 2020;117:6771–6776. doi: 10.1073/pnas.1922083117. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
83. Lo M.K., Jordan R., Arvey A., Sudhamsu J., Shrivastava-Ranjan P., Hotard A.L., Flint M., McMullan L.K., Siegel D., Clarke M.O., et al. GS-5734 and its parent nucleoside analog inhibit Filo-, Pneumo-, and Paramyxoviruses. Sci Rep. 2017;7:43395. doi: 10.1038/srep43395. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
84. Sheahan T.P., Sims A.C., Graham R.L., Menachery V.D., Gralinski L.E., Case J.B., Leist S.R., Pyrc K., Feng J.Y., Trantcheva I., et al. Broad-spectrum antiviral GS-5734 inhibits both epidemic and zoonotic coronaviruses. Sci. Transl. Med. 2017;9 doi: 10.1126/scitranslmed.aal3653. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
85. Sheahan T.P., Sims A.C., Leist S.R., Schafer A., Won J., Brown A.J., Montgomery S.A., Hogg A., Babusis D., Clarke M.O., et al. Comparative therapeutic efficacy of remdesivir and combination lopinavir, ritonavir, and interferon beta against MERS-CoV. Nat. Commun. 2020;11:222. doi: 10.1038/s41467-019-13940-6. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
86. Cardile A.P., Warren T.K., Martins K.A., Reisler R.B., Bavari S. Will There Be a Cure for Ebola? Annu. Rev. Pharmacol. Toxicol. 2017;57:329–348. doi: 10.1146/annurev-pharmtox-010716-105055. [PubMed] [CrossRef] [Google Scholar]
87. Jordan P.C., Liu C., Raynaud P., Lo M.K., Spiropoulou C.F., Symons J.A., Beigelman L., Deval J. Initiation, extension, and termination of RNA synthesis by a paramyxovirus polymerase. PLoS Pathog. 2018;14:e1006889. doi: 10.1371/journal.ppat.1006889. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
88. Tchesnokov E.P., Feng J.Y., Porter D.P., Gotte M. Mechanism of Inhibition of Ebola Virus RNA-Dependent RNA Polymerase by Remdesivir. Viruses. 2019;11:326. doi: 10.3390/v11040326. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
89. Gordon C.J., Tchesnokov E.P., Feng J.Y., Porter D.P., Gotte M. The antiviral compound remdesivir potently inhibits RNA-dependent RNA polymerase from Middle East respiratory syndrome coronavirus. J. Biol. Chem. 2020;295:4773–4779. doi: 10.1074/jbc.AC120.013056. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
90. Holshue M.L., DeBolt C., Lindquist S., Lofy K.H., Wiesman J., Bruce H., Spitters C., Ericson K., Wilkerson S., Tural A., et al. First Case of 2019 Novel Coronavirus in the United States. N. Engl. J. Med. 2020;382:929–936. doi: 10.1056/NEJMoa2001191. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
91. Lai C.C., Shih T.P., Ko W.C., Tang H.J., Hsueh P.R. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and coronavirus disease-2019 (COVID-19): The epidemic and the challenges. Int. J. Antimicrob. Agents. 2020;55:105924. doi: 10.1016/j.ijantimicag.2020.105924. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
92. Ogando N.S., Ferron F., Decroly E., Canard B., Posthuma C.C., Snijder E.J. The Curious Case of the Nidovirus Exoribonuclease: Its Role in RNA Synthesis and Replication Fidelity. Front. Microbiol. 2019;10:1813. doi: 10.3389/fmicb.2019.01813. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
93. Becares M., Pascual-Iglesias A., Nogales A., Sola I., Enjuanes L., Zuniga S. Mutagenesis of Coronavirus nsp14 Reveals Its Potential Role in Modulation of the Innate Immune Response. J. Virol. 2016;90:5399–5414. doi: 10.1128/JVI.03259-15. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
94. Eckerle L.D., Lu X., Sperry S.M., Choi L., Denison M.R. High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants. J. Virol. 2007;81:12135–12144. doi: 10.1128/JVI.01296-07. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
95. Eckerle L.D., Becker M.M., Halpin R.A., Li K., Venter E., Lu X.T., Scherbakova S., Graham R.L., Baric R.S., Stockwell T.B., et al. Infidelity of SARS-CoV Nsp14-Exonuclease Mutant Virus Replication Is Revealed by Complete Genome Sequencing. PLoS Pathog. 2010;6:e1000896. doi: 10.1371/journal.ppat.1000896. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
96. Marcotrigiano J., Gingras A.C., Sonenberg N., Burley S.K. Cocrystal structure of the messenger RNA 5′ cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell. 1997;89:951–961. doi: 10.1016/S0092-8674(00)80280-9. [PubMed] [CrossRef] [Google Scholar]
97. Decroly E., Ferron F., Lescar J., Canard B. Conventional and unconventional mechanisms for capping viral mRNA. Nat. Rev. Microbiol. 2012;10:51–65. doi: 10.1038/nrmicro2675. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
98. Bouvet M., Imbert I., Subissi L., Gluais L., Canard B., Decroly E. RNA 3 ‘-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. Proc. Natl. Acad. Sci. USA. 2012;109:9372–9377. doi: 10.1073/pnas.1201130109. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
99. Derbyshire V., Grindley N.D.F., Joyce C.M. The 3′–5′ Exonuclease of DNA-Polymerase-I of Escherichia-Coli—Contribution of Each Amino-Acid at the Active-Site to the Reaction. EMBO J. 1991;10:17–24. doi: 10.1002/j.1460-2075.1991.tb07916.x. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
100. Romano M., Squeglia F., Berisio R. Structure and Function of RNase AS: A Novel Virulence Factor From Mycobacterium tuberculosis. Curr. Med. Chem. 2015;22:1745–1756. doi: 10.2174/0929867322666150417125301. [PubMed] [CrossRef] [Google Scholar]
101. Romano M., van de Weerd R., Brouwer F.C., Roviello G.N., Lacroix R., Sparrius M., van den Brink-van Stempvoort G., Maaskant J.J., van der Sar A.M., Appelmelk B.J., et al. Structure and function of RNase AS, a polyadenylate-specific exoribonuclease affecting mycobacterial virulence in vivo. Structure. 2014;22:719–730. doi: 10.1016/j.str.2014.01.014. [PubMed] [CrossRef] [Google Scholar]
102. Minskaia E., Hertzig T., Gorbalenya A.E., Campanacci V., Cambillau C., Canard B., Ziebuhr J. Discovery of an RNA virus 3 ‘->
5 ‘ exoribonuclease that is critically involved in coronavirus RNA synthesis. Proc. Natl. Acad. Sci. USA. 2006;103:5108–5113. doi: 10.1073/pnas.0508200103. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
103. Calvanese L., Squeglia F., Romano M., D’Auria G., Falcigno L., Berisio R. Structural and dynamic studies provide insights into specificity and allosteric regulation of ribonuclease as, a key enzyme in mycobacterial virulence. J. Biomol. Struct. Dyn. 2019:1–13. doi: 10.1080/07391102.2019.1643786. [PubMed] [CrossRef] [Google Scholar]
104. Denison M.R., Graham R.L., Donaldson E.F., Eckerle L.D., Baric R.S. Coronaviruses an RNA proofreading machine regulates replication fidelity and diversity. RNA Biol. 2011;8:270–279. doi: 10.4161/rna.8.2.15013. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
105. Tchesnokov E.P., Obikhod A., Schinazi R.F., Gotte M. Delayed chain termination protects the anti-hepatitis B virus drug entecavir from excision by HIV-1 reverse transcriptase. J. Biol. Chem. 2008;283:34218–34228. doi: 10.1074/jbc.M806797200. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
106. Dulin D., Arnold J.J., van Laar T., Oh H.S., Lee C., Perkins A.L., Harki D.A., Depken M., Cameron C.E., Dekker N.H. Signatures of Nucleotide Analog Incorporation by an RNA-Dependent RNA Polymerase Revealed Using High-Throughput Magnetic Tweezers. Cell Rep. 2017;21:1063–1076. doi: 10.1016/j.celrep.2017.10.005. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
107. Smith E.C., Blanc H., Surdel M.C., Vignuzzi M., Denison M.R. Coronaviruses lacking exoribonuclease activity are susceptible to lethal mutagenesis: Evidence for proofreading and potential therapeutics. PLoS Pathog. 2013;9:e1003565. doi: 10.1371/journal.ppat.1003565. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
108. Morse J.S., Lalonde T., Xu S., Liu W.R. Learning from the Past: Possible Urgent Prevention and Treatment Options for Severe Acute Respiratory Infections Caused by 2019-nCoV. Chembiochem. 2020;21:730–738. doi: 10.1002/cbic.202000047. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
109. Rao S.T., Rossmann M.G. Comparison of super-secondary structures in proteins. J. Mol. Biol. 1973;76:241–256. doi: 10.1016/0022-2836(73)90388-4. [PubMed] [CrossRef] [Google Scholar]
110. Byszewska M., Smietanski M., Purta E., Bujnicki J.M. RNA methyltransferases involved in 5′ cap biosynthesis. RNA Biol. 2014;11:1597–1607. doi: 10.1080/15476286.2015.1004955. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
111. Chouhan B.P.S., Maimaiti S., Gade M., Laurino P. Rossmann-Fold Methyltransferases: Taking a “beta-Turn” around Their Cofactor, S-Adenosylmethionine. Biochemistry. 2019;58:166–170. doi: 10.1021/acs.biochem.8b00994. [PubMed] [CrossRef] [Google Scholar]
112. Schubert H.L., Blumenthal R.M., Cheng X.D. Many paths to methyltransfer: A chronicle of convergence. Trends Biochem. Sci. 2003;28:329–335. doi: 10.1016/S0968-0004(03)00090-2. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
113. Chen Y., Cai H., Pan J., Xiang N., Tien P., Ahola T., Guo D.Y. Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase. Proc. Natl. Acad. Sci. USA. 2009;106:3484–3489. doi: 10.1073/pnas.0808790106. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
114. Chen Y., Tao J.L., Sun Y., Wu A.D., Su C.Y., Gao G.Z., Cai H., Qiu S., Wu Y.L., Ahola T., et al. Structure-Function Analysis of Severe Acute Respiratory Syndrome Coronavirus RNA Cap Guanine-N7-Methyltransferase. J. Virol. 2013;87:6296–6305. doi: 10.1128/JVI.00061-13. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
115. Jin X., Chen Y., Sun Y., Zeng C., Wang Y., Tao J.L., Wu A.D., Yu X., Zhang Z., Tian J., et al. Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP. Virus Res. 2013;176:45–52. doi: 10.1016/j.virusres.2013.05.001. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
116. Jankowsky E., Fairman M.E. RNA helicases-one fold for many functions. Curr. Opin. Struct. Biol. 2007;17:316–324. doi: 10.1016/j.sbi.2007.05.007. [PubMed] [CrossRef] [Google Scholar]
117. Deng Z., Lehmann K.C., Li X., Feng C., Wang G., Zhang Q., Qi X., Yu L., Zhang X., Feng W., et al. Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase. Nucleic Acids Res. 2014;42:3464–3477. doi: 10.1093/nar/gkt1310. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
118. Ivanov K.A., Ziebuhr J. Human coronavirus 229E nonstructural protein 13: Characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5′-triphosphatase activities. J. Virol. 2004;78:7833–7838. doi: 10.1128/JVI.78.14.7833-7838.2004. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
119. Adedeji A.O., Lazarus H. Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase. mSphere. 2016;1:e00235-16. doi: 10.1128/mSphere.00235-16. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
120. Adedeji A.O., Marchand B., Te Velthuis A.J., Snijder E.J., Weiss S., Eoff R.L., Singh K., Sarafianos S.G. Mechanism of nucleic acid unwinding by SARS-CoV helicase. PLoS ONE. 2012;7:e36521. doi: 10.1371/journal.pone.0036521. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
121. Ziebuhr J. The coronavirus replicase. Curr. Top Microbiol. Immunol. 2005;287:57–94. doi: 10.1007/3-540-26765-4_3. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
122. Van Dinten L.C., van Tol H., Gorbalenya A.E., Snijder E.J. The predicted metal-binding region of the arterivirus helicase protein is involved in subgenomic mRNA synthesis, genome replication, and virion biogenesis. J. Virol. 2000;74:5213–5223. doi: 10.1128/JVI.74.11.5213-5223.2000. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
123. Adedeji A.O., Singh K., Calcaterra N.E., DeDiego M.L., Enjuanes L., Weiss S., Sarafianos S.G. Severe acute respiratory syndrome coronavirus replication inhibitor that interferes with the nucleic acid unwinding of the viral helicase. Antimicrob. Agents Chemother. 2012;56:4718–4728. doi: 10.1128/AAC.00957-12. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
124. Adedeji A.O., Singh K., Kassim A., Coleman C.M., Elliott R., Weiss S.R., Frieman M.B., Sarafianos S.G. Evaluation of SSYA10-001 as a replication inhibitor of severe acute respiratory syndrome, mouse hepatitis, and Middle East respiratory syndrome coronaviruses. Antimicrob. Agents Chemother. 2014;58:4894–4898. doi: 10.1128/AAC.02994-14. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
125. Aouadi W., Blanjoie A., Vasseur J.J., Debart F., Canard B., Decroly E. Binding of the Methyl Donor S-Adenosyl-L-Methionine to Middle East Respiratory Syndrome Coronavirus 2 ‘-O-Methyltransferase nsp16 Promotes Recruitment of the Allosteric Activator nsp10. J. Virol. 2017;91:e02217-16. doi: 10.1128/JVI.02217-16. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
126. Martin J.L., McMillan F.M. SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold. Curr. Opin. Struc. Biol. 2002;12:783–793. doi: 10.1016/S0959-440X(02)00391-3. [PubMed] [CrossRef] [Google Scholar]
127. Joseph J.S., Saikatendu K.S., Subramanian V., Neuman B.W., Brooun A., Griffith M., Moy K., Yadav M.K., Velasquez J., Buchmeier M.J., et al. Crystal structure of nonstructural protein 10 from the severe acute respiratory syndrome coronavirus reveals a novel fold with two zinc-binding motifs. J. Virol. 2006;80:7894–7901. doi: 10.1128/JVI.00467-06. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
128. Matthes N., Mesters J.R., Coutard B., Canard B., Snijder E.J., Moll R., Hilgenfeld R. The non-structural protein Nsp10 of mouse hepatitis virus binds zinc ions and nucleic acids. FEBS Lett. 2006;580:4143–4149. doi: 10.1016/j.febslet.2006.06.061. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
129. Zust R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., Szretter K.J., Baker S.C., Barchet W., Diamond M.S., et al. Ribose 2’-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5. Nat. Immunol. 2011;12:137–143. doi: 10.1038/ni.1979. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
130. Devarkar S.C., Wang C., Miller M.T., Ramanathan A., Jiang F., Khan A.G., Patel S.S., Marcotrigiano J. Structural basis for m7G recognition and 2’-O-methyl discrimination in capped RNAs by the innate immune receptor RIG-I. Proc. Natl. Acad. Sci. USA. 2016;113:596–601. doi: 10.1073/pnas.1515152113. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
131. Hyde J.L., Diamond M.S. Innate immune restriction and antagonism of viral RNA lacking 2-O methylation. Virology. 2015;479–480:66–74. doi: 10.1016/j.virol.2015.01.019. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
132. Daffis S., Szretter K.J., Schriewer J., Li J., Youn S., Errett J., Lin T.Y., Schneller S., Zust R., Dong H., et al. 2’-O methylation of the viral mRNA cap evades host restriction by IFIT family members. Nature. 2010;468:452–456. doi: 10.1038/nature09489. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
133. Diamond M.S., Farzan M. The broad-spectrum antiviral functions of IFIT and IFITM proteins. Nat. Rev. Immunol. 2013;13:46–57. doi: 10.1038/nri3344. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
1. Zhou P., Yang X.L., Wang X.G., Hu B., Zhang L., Zhang W., Si H.R., Zhu Y., Li B., Huang C.L., et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin. Nature. 2020;579:270–273. doi: 10.1038/s41586-020-2012-7. [PMC free article] [PubMed] [CrossRef] [Google Scholar]
A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping
The current coronavirus disease-2019 (COVID-19) pandemic is due to the novel coronavirus SARS-CoV-2. The scientific community has mounted a strong response by accelerating research and innovation, and has quickly set the foundation for understanding the molecular determinants of the disease for the development of targeted therapeutic interventions. The replication of the viral genome within the infected cells is a key stage of the SARS-CoV-2 life cycle. It is a complex process involving the action of several viral and host proteins in order to perform RNA polymerization, proofreading and final capping. This review provides an update of the structural and functional data on the key actors of the replicatory machinery of SARS-CoV-2, to fill the gaps in the currently available structural data, which is mainly obtained through homology modeling. Moreover, learning from similar viruses, we collect data from the literature to reconstruct the pattern of interactions among the protein actors of the SARS-CoV-2 RNA polymerase machinery. Here, an important role is played by co-factors such as Nsp8 and Nsp10, not only as allosteric activators but also as molecular connectors that hold the entire machinery together to enhance the efficiency of RNA replication.
The current coronavirus disease-2019 (COVID-19) pandemic is due to the novel coronavirus SARS-CoV-2. The scientific community has mounted a strong response by accelerating research and innovation, and has quickly set the foundation for understanding the molecular determinants of the disease for the development of targeted therapeutic interventions. The replication of the viral genome within the infected cells is a key stage of the SARS-CoV-2 life cycle. It is a complex process involving the action of several viral and host proteins in order to perform RNA polymerization, proofreading and final capping. This review provides an update of the structural and functional data on the key actors of the replicatory machinery of SARS-CoV-2, to fill the gaps in the currently available structural data, which is mainly obtained through homology modeling. Moreover, learning from similar viruses, we collect data from the literature to reconstruct the pattern of interactions among the protein actors of the SARS-CoV-2 RNA polymerase machinery. Here, an important role is played by co-factors such as Nsp8 and Nsp10, not only as allosteric activators but also as molecular connectors that hold the entire machinery together to enhance the efficiency of RNA replication.
A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping
A Structural View of SARS-CoV-2 RNA Replication Machinery: RNA Synthesis, Proofreading and Final Capping
Other filter: ([btitle,keywords] "Sars-Cov-2" OR [btit ...
Autiero I, Roviello GN
* Interaction of Laurusides 1 and 2 with the 3C-like Protease (Mpro) from Wild-Type and Omicron Variant of SARS-CoV-2: A Molecular Dynamics Study (5 views)
International Journal Of Molecular Sciences, 2023 Mar; 25: 5511-5511.
Impact Factor: 6.208
View Export to BibTeX Export to EndNote
Ricci A, Roviello GN
* Exploring the Protective Effect of Food Drugs against Viral Diseases: Interaction of Functional Food Ingredients and SARS-CoV-2, Influenza Virus, and HSV (9 views)
Life, 2023 Feb; 13: 402-417.
Impact Factor: 3.253
View Export to BibTeX Export to EndNote
Vicidomini C, Roviello GN
* Potential Anti-SARS-CoV-2 Molecular Strategies (10 views)
Molecules, 2023 Feb; 28: 2118-2123.
Impact Factor: 4.9
View Export to BibTeX Export to EndNote
Berisio R
* Understanding Molecular Actors of SARS-CoV-2 Virulence to Tackle COVID-19 Outbreak (7 views)
Cells (ISSN: 2073-4409linking), 2022 Nov 14; 11(22): N/D-N/D.
Impact Factor: 7.7
View Export to BibTeX Export to EndNote
Squeglia F, Romano M, Esposito L, Barra G, Campiglia P, Sala M, Scala MC, Ruggiero A, Berisio R
* Structure-Based Development of SARS-CoV-2 Spike Interactors (9 views)
Int J Mol Sci (ISSN: 1422-0067linking), 2022 May 17; 23(10): N/D-N/D.
Impact Factor: 6.21
View Export to BibTeX Export to EndNote
Roviello V, Scognamiglio PL, Caruso U, Vicidomini C, Roviello GN
* Evaluating In Silico the Potential Health and Environmental Benefits of Houseplant Volatile Organic Compounds for an Emerging 'Indoor Forest Bathing' Approach (34 views)
Int J Environ Res Public Health (ISSN: 1660-4601linking), 2022 Jan 16; 19(1): 273-273.
Impact Factor: 3.39
View Export to BibTeX Export to EndNote
Costanzo M, De Giglio MAR, Roviello GN
* Anti-Coronavirus Vaccines: Past Investigations on SARS-CoV-1 and MERS-CoV, the Approved Vaccines from BioNTech/Pfizer, Moderna, Oxford/AstraZeneca and others under Development Against SARSCoV- 2 Infection (5 views)
Curr Med Chem (ISSN: 0929-8673linking), 2022; 29 (1 ): 4-18.
Impact Factor:
View Export to BibTeX Export to EndNote
Roviello V, Roviello GN
* Less COVID-19 deaths in southern and insular Italy explained by forest bathing, Mediterranean environment, and antiviral plant volatile organic compounds (20 views)
Environ Chem Lett (ISSN: 1610-3653linking), 2022; 20(1): 7-17.
Impact Factor: 13.615
View Export to BibTeX Export to EndNote
Balasco N, Damaggio G, Esposito L, Villani F, Berisio R, Colonna V, Vitagliano L
* A global analysis of conservative and non-conservative mutations in SARS-CoV-2 detected in the first year of the COVID-19 world-wide diffusion (5 views)
Sci Rep (ISSN: 2045-2322linking), 2021 Dec 30; 11(1): 24495-24495.
Impact Factor: 5.078
View Export to BibTeX Export to EndNote
Megna R
* Inferring a cause-effect relationship between lockdown restrictions and COVID-19 pandemic trend during the first wave (84 views)
Health Policy (ISSN: 0168-8510, 0168-8510linking), 2021 Nov; 125(11): 1441-1447.
Impact Factor: 2.98
View Export to BibTeX Export to EndNote
Roviello V, Roviello GN
* Less COVID-19 deaths in southern and insular Italy explained by forest bathing, Mediterranean environment, and antiviral plant volatile organic compounds (34 views)
Environ Chem Lett (ISSN: 1610-3653linking), 2021 Nov; N/D: 1-11.
Impact Factor: 9.027
View Export to BibTeX Export to EndNote
Testino G, Di Biagio A, Fagoonee S, Pellicano R
* SARS-CoV-2, alcohol consumption and liver injury (8 views)
Minerva Med (ISSN: 0026-4806linking), 2021 Oct 21; N/D: N/D-N/D.
Impact Factor: 4.806
View Export to BibTeX Export to EndNote
Capasso D, Di Gaetano S, Selvaraj C, Pedone E
* Editorial: Molecular Studies of Covid-19 Chemistry (22 views)
Front Chem (ISSN: 2296-2646linking), 2021 Aug 31; 9: 729142-729142.
Impact Factor: 4.62
View Export to BibTeX Export to EndNote
Sadremomtaz A, Al-dahmani ZM, Ruiz-moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-velázquez MA, De Jong D, De Jonge J, Smit J, Dömling A, Van Goor H, Groves MR
* Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein (6 views)
J Med Chem (ISSN: 0022-2623linking), 2021 Jul 30; N/D: N/D-N/D.
Impact Factor:
View Export to BibTeX Export to EndNote
Perrella F, Coppola F, Petrone A, Platella C, Montesarchio D, Stringaro A, Ravagnan G, Fuggetta MP, Rega N, Musumeci D
* Interference of Polydatin/Resveratrol in the ACE2: Spike Recognition during COVID-19 Infection. A Focus on Their Potential Mechanism of Action through Computational and Biochemical Assays (15 views)
Biomolecules (ISSN: 2218-273xlinking), 2021 Jul 16; 11(7): N/D-N/D.
Impact Factor: 4.57
View Export to BibTeX Export to EndNote
Roviello V, Musumeci D, Mokhir A, Roviello GN
* Evidence of Protein Binding by a Nucleopeptide Based on a Thyminedecorated L-Diaminopropanoic Acid through CD and In Silico Studies (26 views) (PDF 12 views)
Curr Med Chem (ISSN: 0929-8673linking), 2021 Jul; 28(24): 5004-5015.
Impact Factor: 4.53
View Export to BibTeX Export to EndNote
Vicidomini C, Roviello V, Roviello GN
* In Silico Investigation on the Interaction of Chiral Phytochemicals from Opuntia ficus-indica with SARS-CoV-2 Mpro (15 views)
Symmetry, 2021 Jul; 13: 1041-1048.
Impact Factor: 2.713
View Export to BibTeX Export to EndNote
Di Gaetano S, Capasso D, Delre P, Pirone L, Saviano M, Pedone E, Mangiatordi GF
* More Is Always Better Than One: The N-Terminal Domain of the Spike Protein as Another Emerging Target for Hampering the SARS-CoV-2 Attachment to Host Cells (27 views)
Int J Mol Sci (ISSN: 1422-0067linking), 2021 Jun 16; 22 (12 ): N/D-N/D.
Impact Factor:
View Export to BibTeX Export to EndNote
Costanzo M, De Giglio MAR, Roviello GN
* Anti-Coronavirus Vaccines: Past Investigations on SARS-CoV-1 and MERS-CoV, the Approved Vaccines from BioNTech/Pfizer, Moderna, Oxford/AstraZeneca and others under Development Against SARS-CoV-2 Infection (27 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021 May 21; DOI:10.2174/09298673: 1-1.
Impact Factor: 4.53
View Export to BibTeX Export to EndNote
Tito A, Colantuono C, Pirone L, Pedone E, Intartaglia D, Giamundo G, Conte I, Vitaglione P, Apone F
* Pomegranate Peel Extract as an Inhibitor of SARS-CoV-2 Spike Binding to Human ACE2 Receptor (in vitro): A Promising Source of Novel Antiviral Drugs (42 views) (PDF 18 views)
Front Chem (ISSN: 2296-2646linking), 2021 Apr 28; 9: 638187-638187.
Impact Factor: 3.693
View Export to BibTeX Export to EndNote
Vicidomini C, Roviello V, Roviello GN
* Molecular Basis of the Therapeutical Potential of Clove (Syzygium aromaticum L. ) and Clues to Its Anti-COVID-19 Utility (78 views)
Molecules (ISSN: 1420-3049linking, 1420-3049electronic), 2021 Mar 26; 26(7): 1880-1886.
Impact Factor: 4.411
View Export to BibTeX Export to EndNote
Borbone N, Piccialli G, Roviello GN, Oliviero G
* Nucleoside Analogs and Nucleoside Precursors as Drugs in the Fight against SARS-CoV-2 and Other Coronaviruses (109 views)
Molecules (ISSN: 1420-3049linking, 1420-3049electronic), 2021 Feb 13; 26(4): 986-1002.
Impact Factor: 4.411
View Export to BibTeX Export to EndNote
Actis GC, Ribaldone DG, Fagoonee S, Pellicano R
* COVID-19: a user's guide, status of the art, and an original proposal to terminate viral recurrence (99 views)
Hepatology (ISSN: 0026-4806linking, 1827-1669electronic), 2021 Feb; 112(1): 144-152.
Impact Factor: 3.031
View Export to BibTeX Export to EndNote
Nappi C, Megna R, Acampa W, Assante R, Zampella E, Gaudieri V, Mannarino T, Green R, Cantoni V, Petretta M, Cuocolo A
* Effects of the COVID-19 pandemic on myocardial perfusion imaging for ischemic heart disease (65 views)
Eur J Nucl Med (ISSN: 1619-7070linking, 1619-7070print, 1619-7089electronic), 2021 Feb; 48(2): 421-427.
Impact Factor: 7.081
View Export to BibTeX Export to EndNote
Roviello V, Roviello GN
* Lower COVID-19 mortality in Italian forested areas suggests immunoprotection by Mediterranean plants (179 views)
Environ Chem Lett (ISSN: 1610-3653linking), 2021 Jan; 19: 699-710.
Impact Factor: 9.027
View Export to BibTeX Export to EndNote
Ponsiglione A, Nappi C, Imbriaco M, Ascione R, Megna R, Petretta M, Cuocolo A
* Cardiac magnetic resonance imaging during the COVID-19 pandemic: A southern Italian single-center experience (84 views)
Eur J Radiol Open (ISSN: 2352-0477electronic, 2352-0477linking), 2021; 8: 100319-100319.
Impact Factor: 0.654
View Export to BibTeX Export to EndNote
Vincenzi M, Mercurio FA, Leone M
* NMR spectroscopy in the conformational analysis of peptides: an overview (91 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021; 28(14): 2729-2782.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Vincenzi M, Leone M
* The fight against human viruses: how NMR can help (64 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021; 28(22): 4380-4453.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Squeglia F, Romano M, Ruggiero A, Maga G, Berisio R
* Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins (81 views)
Front Chem (ISSN: 2296-2646linking), 2020 Dec 10; 8: 602162-602162.
Impact Factor: 3.693
View Export to BibTeX Export to EndNote
Megna R
* First month of the epidemic caused by COVID-19 in Italy: current status and real-time outbreak development forecast (283 views)
Glob Health Res Policy (ISSN: 2397-0642linking), 2020 Oct 1; 5: 43-43.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Cella L, Gagliardi G, Hedman M, Palma G
* Injuries From Asymptomatic COVID-19 Disease: New Hidden Toxicity Risk Factors in Thoracic Radiation Therapy (63 views) (PDF 17 views)
Int J Radiat Oncol (ISSN: 0360-3016linking, 1879-355x), 2020 Oct 1; 108(2): 394-396.
Impact Factor: 5.859
View Export to BibTeX Export to EndNote
Pirone L, Del Gatto A, Di Gaetano S, Saviano M, Capasso D, Zaccaro L, Pedone E
* A Multi-Targeting Approach to Fight SARS-CoV-2 Attachment (526 views) (PDF 128 views)
Front Mol Biosci (ISSN: 2296-889xlinking), 2020 Aug 3; 7: 186-186.
Impact Factor: 4.188
View Export to BibTeX Export to EndNote
Scarpellini E, Fagoonee S, Rinninella E, Rasetti C, Aquila I, Larussa T, Ricci P, Luzza F, Abenavoli L
* Gut Microbiota and Liver Interaction through Immune System Cross-Talk: A Comprehensive Review at the Time of the SARS-CoV-2 Pandemic (64 views)
J Clin Med (ISSN: 2077-0383linking, 2077-0383electronic), 2020 Aug 3; 9(8): N/D-N/D.
Impact Factor: 6.78
View Export to BibTeX Export to EndNote
Testino G, Fagoonee S
* Coronavirus disease 2019 outbreak: liver disease a prognostic tool? (97 views)
Panminerva Med (ISSN: 0031-0808linking, 1827-1898electronic), 2020 May 14; N/D: N/D-N/D.
Impact Factor: 3.467
View Export to BibTeX Export to EndNote
D'Andrea A, Radmilovic J, Carbone A, Forni A, Tagliamonte E, Riegler L, Liccardo B, Crescibene F, Sirignano C, Esposito G, Bossone E
* Multimodality imaging in COVID-19 patients: A key role from diagnosis to prognosis (78 views) (PDF 11 views)
World Journal Of Radiology, 2020 May; 21(5): 345-353.
Impact Factor: 0.57
View Export to BibTeX Export to EndNote
Costanzo M, De Giglio MAR, Roviello GN
* SARS-CoV-2: Recent Reports on Antiviral Therapies Based on Lopinavir/Ritonavir, Darunavir/Umifenovir, Hydroxychloroquine, Remdesivir, Favipiravir and other Drugs for the Treatment of the New Coronavirus (298 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2020 Apr 16; 27(27): 4536-4541.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Vincenzi M, Mercurio FA, Leone M
* Protein Interaction Domains and Post-Translational Modifications: Structural Features and Drug Discovery Applications (80 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2020; 27(37): 6306-6355.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Vincenzi M, Mercurio FA, Leone M
* Sam Domains in Multiple Diseases (237 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2020; 27(3): 450-476.
Impact Factor: 3.469
View Export to BibTeX Export to EndNote
Balasco N, Barone D, Sandomenico A, Ruggiero A, Doti N, Berisio R, Ruvo M, Vitagliano L
* Structural Versatility of Hepatitis C Virus Proteins: Implications for the Design of Novel Anti-HCV Intervention Strategies (290 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2017 Nov 24; 24(36): 4081-4101.
Impact Factor: 3.469
View Export to BibTeX Export to EndNote
De Rosa L, Romanelli A, D'Andrea LD
* Chemical ligation in Structural Biology in “Chemical Ligation: Tools for Biomolecules Synthesis and Modification” (286 views)
John Wiley & Sons, 2017; N/D: N/D-N/D.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Lanza V, Travaglia A, Malgieri G, Fattorusso R, GrassoG, Di Natale G, Zito V, Arena G, Milardi D, Rizzarelli E
* Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions (279 views) (PDF 172 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2016 Dec 05; 22(49): 17767-17775.
Impact Factor: 5.317
View Export to BibTeX Export to EndNote
Vergara A, Lorber B, Sauter C, Giege R, Zagari A
* Lessons from crystals grown in the Advanced Protein Crystallisation Facility for conventional crystallisation applied to structural biology (369 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005; 118(2-3): 102-112.
Impact Factor: 1.925
View Export to BibTeX Export to EndNote
* Interaction of Laurusides 1 and 2 with the 3C-like Protease (Mpro) from Wild-Type and Omicron Variant of SARS-CoV-2: A Molecular Dynamics Study (5 views)
International Journal Of Molecular Sciences, 2023 Mar; 25: 5511-5511.
Impact Factor: 6.208
View Export to BibTeX Export to EndNote
Ricci A, Roviello GN
* Exploring the Protective Effect of Food Drugs against Viral Diseases: Interaction of Functional Food Ingredients and SARS-CoV-2, Influenza Virus, and HSV (9 views)
Life, 2023 Feb; 13: 402-417.
Impact Factor: 3.253
View Export to BibTeX Export to EndNote
Vicidomini C, Roviello GN
* Potential Anti-SARS-CoV-2 Molecular Strategies (10 views)
Molecules, 2023 Feb; 28: 2118-2123.
Impact Factor: 4.9
View Export to BibTeX Export to EndNote
Berisio R
* Understanding Molecular Actors of SARS-CoV-2 Virulence to Tackle COVID-19 Outbreak (7 views)
Cells (ISSN: 2073-4409linking), 2022 Nov 14; 11(22): N/D-N/D.
Impact Factor: 7.7
View Export to BibTeX Export to EndNote
Squeglia F, Romano M, Esposito L, Barra G, Campiglia P, Sala M, Scala MC, Ruggiero A, Berisio R
* Structure-Based Development of SARS-CoV-2 Spike Interactors (9 views)
Int J Mol Sci (ISSN: 1422-0067linking), 2022 May 17; 23(10): N/D-N/D.
Impact Factor: 6.21
View Export to BibTeX Export to EndNote
Roviello V, Scognamiglio PL, Caruso U, Vicidomini C, Roviello GN
* Evaluating In Silico the Potential Health and Environmental Benefits of Houseplant Volatile Organic Compounds for an Emerging 'Indoor Forest Bathing' Approach (34 views)
Int J Environ Res Public Health (ISSN: 1660-4601linking), 2022 Jan 16; 19(1): 273-273.
Impact Factor: 3.39
View Export to BibTeX Export to EndNote
Costanzo M, De Giglio MAR, Roviello GN
* Anti-Coronavirus Vaccines: Past Investigations on SARS-CoV-1 and MERS-CoV, the Approved Vaccines from BioNTech/Pfizer, Moderna, Oxford/AstraZeneca and others under Development Against SARSCoV- 2 Infection (5 views)
Curr Med Chem (ISSN: 0929-8673linking), 2022; 29 (1 ): 4-18.
Impact Factor:
View Export to BibTeX Export to EndNote
Roviello V, Roviello GN
* Less COVID-19 deaths in southern and insular Italy explained by forest bathing, Mediterranean environment, and antiviral plant volatile organic compounds (20 views)
Environ Chem Lett (ISSN: 1610-3653linking), 2022; 20(1): 7-17.
Impact Factor: 13.615
View Export to BibTeX Export to EndNote
Balasco N, Damaggio G, Esposito L, Villani F, Berisio R, Colonna V, Vitagliano L
* A global analysis of conservative and non-conservative mutations in SARS-CoV-2 detected in the first year of the COVID-19 world-wide diffusion (5 views)
Sci Rep (ISSN: 2045-2322linking), 2021 Dec 30; 11(1): 24495-24495.
Impact Factor: 5.078
View Export to BibTeX Export to EndNote
Megna R
* Inferring a cause-effect relationship between lockdown restrictions and COVID-19 pandemic trend during the first wave (84 views)
Health Policy (ISSN: 0168-8510, 0168-8510linking), 2021 Nov; 125(11): 1441-1447.
Impact Factor: 2.98
View Export to BibTeX Export to EndNote
Roviello V, Roviello GN
* Less COVID-19 deaths in southern and insular Italy explained by forest bathing, Mediterranean environment, and antiviral plant volatile organic compounds (34 views)
Environ Chem Lett (ISSN: 1610-3653linking), 2021 Nov; N/D: 1-11.
Impact Factor: 9.027
View Export to BibTeX Export to EndNote
Testino G, Di Biagio A, Fagoonee S, Pellicano R
* SARS-CoV-2, alcohol consumption and liver injury (8 views)
Minerva Med (ISSN: 0026-4806linking), 2021 Oct 21; N/D: N/D-N/D.
Impact Factor: 4.806
View Export to BibTeX Export to EndNote
Capasso D, Di Gaetano S, Selvaraj C, Pedone E
* Editorial: Molecular Studies of Covid-19 Chemistry (22 views)
Front Chem (ISSN: 2296-2646linking), 2021 Aug 31; 9: 729142-729142.
Impact Factor: 4.62
View Export to BibTeX Export to EndNote
Sadremomtaz A, Al-dahmani ZM, Ruiz-moreno AJ, Monti A, Wang C, Azad T, Bell JC, Doti N, Velasco-velázquez MA, De Jong D, De Jonge J, Smit J, Dömling A, Van Goor H, Groves MR
* Synthetic Peptides That Antagonize the Angiotensin-Converting Enzyme-2 (ACE-2) Interaction with SARS-CoV-2 Receptor Binding Spike Protein (6 views)
J Med Chem (ISSN: 0022-2623linking), 2021 Jul 30; N/D: N/D-N/D.
Impact Factor:
View Export to BibTeX Export to EndNote
Perrella F, Coppola F, Petrone A, Platella C, Montesarchio D, Stringaro A, Ravagnan G, Fuggetta MP, Rega N, Musumeci D
* Interference of Polydatin/Resveratrol in the ACE2: Spike Recognition during COVID-19 Infection. A Focus on Their Potential Mechanism of Action through Computational and Biochemical Assays (15 views)
Biomolecules (ISSN: 2218-273xlinking), 2021 Jul 16; 11(7): N/D-N/D.
Impact Factor: 4.57
View Export to BibTeX Export to EndNote
Roviello V, Musumeci D, Mokhir A, Roviello GN
* Evidence of Protein Binding by a Nucleopeptide Based on a Thyminedecorated L-Diaminopropanoic Acid through CD and In Silico Studies (26 views) (PDF 12 views)
Curr Med Chem (ISSN: 0929-8673linking), 2021 Jul; 28(24): 5004-5015.
Impact Factor: 4.53
View Export to BibTeX Export to EndNote
Vicidomini C, Roviello V, Roviello GN
* In Silico Investigation on the Interaction of Chiral Phytochemicals from Opuntia ficus-indica with SARS-CoV-2 Mpro (15 views)
Symmetry, 2021 Jul; 13: 1041-1048.
Impact Factor: 2.713
View Export to BibTeX Export to EndNote
Di Gaetano S, Capasso D, Delre P, Pirone L, Saviano M, Pedone E, Mangiatordi GF
* More Is Always Better Than One: The N-Terminal Domain of the Spike Protein as Another Emerging Target for Hampering the SARS-CoV-2 Attachment to Host Cells (27 views)
Int J Mol Sci (ISSN: 1422-0067linking), 2021 Jun 16; 22 (12 ): N/D-N/D.
Impact Factor:
View Export to BibTeX Export to EndNote
Costanzo M, De Giglio MAR, Roviello GN
* Anti-Coronavirus Vaccines: Past Investigations on SARS-CoV-1 and MERS-CoV, the Approved Vaccines from BioNTech/Pfizer, Moderna, Oxford/AstraZeneca and others under Development Against SARS-CoV-2 Infection (27 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021 May 21; DOI:10.2174/09298673: 1-1.
Impact Factor: 4.53
View Export to BibTeX Export to EndNote
Tito A, Colantuono C, Pirone L, Pedone E, Intartaglia D, Giamundo G, Conte I, Vitaglione P, Apone F
* Pomegranate Peel Extract as an Inhibitor of SARS-CoV-2 Spike Binding to Human ACE2 Receptor (in vitro): A Promising Source of Novel Antiviral Drugs (42 views) (PDF 18 views)
Front Chem (ISSN: 2296-2646linking), 2021 Apr 28; 9: 638187-638187.
Impact Factor: 3.693
View Export to BibTeX Export to EndNote
Vicidomini C, Roviello V, Roviello GN
* Molecular Basis of the Therapeutical Potential of Clove (Syzygium aromaticum L. ) and Clues to Its Anti-COVID-19 Utility (78 views)
Molecules (ISSN: 1420-3049linking, 1420-3049electronic), 2021 Mar 26; 26(7): 1880-1886.
Impact Factor: 4.411
View Export to BibTeX Export to EndNote
Borbone N, Piccialli G, Roviello GN, Oliviero G
* Nucleoside Analogs and Nucleoside Precursors as Drugs in the Fight against SARS-CoV-2 and Other Coronaviruses (109 views)
Molecules (ISSN: 1420-3049linking, 1420-3049electronic), 2021 Feb 13; 26(4): 986-1002.
Impact Factor: 4.411
View Export to BibTeX Export to EndNote
Actis GC, Ribaldone DG, Fagoonee S, Pellicano R
* COVID-19: a user's guide, status of the art, and an original proposal to terminate viral recurrence (99 views)
Hepatology (ISSN: 0026-4806linking, 1827-1669electronic), 2021 Feb; 112(1): 144-152.
Impact Factor: 3.031
View Export to BibTeX Export to EndNote
Nappi C, Megna R, Acampa W, Assante R, Zampella E, Gaudieri V, Mannarino T, Green R, Cantoni V, Petretta M, Cuocolo A
* Effects of the COVID-19 pandemic on myocardial perfusion imaging for ischemic heart disease (65 views)
Eur J Nucl Med (ISSN: 1619-7070linking, 1619-7070print, 1619-7089electronic), 2021 Feb; 48(2): 421-427.
Impact Factor: 7.081
View Export to BibTeX Export to EndNote
Roviello V, Roviello GN
* Lower COVID-19 mortality in Italian forested areas suggests immunoprotection by Mediterranean plants (179 views)
Environ Chem Lett (ISSN: 1610-3653linking), 2021 Jan; 19: 699-710.
Impact Factor: 9.027
View Export to BibTeX Export to EndNote
Ponsiglione A, Nappi C, Imbriaco M, Ascione R, Megna R, Petretta M, Cuocolo A
* Cardiac magnetic resonance imaging during the COVID-19 pandemic: A southern Italian single-center experience (84 views)
Eur J Radiol Open (ISSN: 2352-0477electronic, 2352-0477linking), 2021; 8: 100319-100319.
Impact Factor: 0.654
View Export to BibTeX Export to EndNote
Vincenzi M, Mercurio FA, Leone M
* NMR spectroscopy in the conformational analysis of peptides: an overview (91 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021; 28(14): 2729-2782.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Vincenzi M, Leone M
* The fight against human viruses: how NMR can help (64 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021; 28(22): 4380-4453.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Squeglia F, Romano M, Ruggiero A, Maga G, Berisio R
* Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins (81 views)
Front Chem (ISSN: 2296-2646linking), 2020 Dec 10; 8: 602162-602162.
Impact Factor: 3.693
View Export to BibTeX Export to EndNote
Megna R
* First month of the epidemic caused by COVID-19 in Italy: current status and real-time outbreak development forecast (283 views)
Glob Health Res Policy (ISSN: 2397-0642linking), 2020 Oct 1; 5: 43-43.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Cella L, Gagliardi G, Hedman M, Palma G
* Injuries From Asymptomatic COVID-19 Disease: New Hidden Toxicity Risk Factors in Thoracic Radiation Therapy (63 views) (PDF 17 views)
Int J Radiat Oncol (ISSN: 0360-3016linking, 1879-355x), 2020 Oct 1; 108(2): 394-396.
Impact Factor: 5.859
View Export to BibTeX Export to EndNote
Pirone L, Del Gatto A, Di Gaetano S, Saviano M, Capasso D, Zaccaro L, Pedone E
* A Multi-Targeting Approach to Fight SARS-CoV-2 Attachment (526 views) (PDF 128 views)
Front Mol Biosci (ISSN: 2296-889xlinking), 2020 Aug 3; 7: 186-186.
Impact Factor: 4.188
View Export to BibTeX Export to EndNote
Scarpellini E, Fagoonee S, Rinninella E, Rasetti C, Aquila I, Larussa T, Ricci P, Luzza F, Abenavoli L
* Gut Microbiota and Liver Interaction through Immune System Cross-Talk: A Comprehensive Review at the Time of the SARS-CoV-2 Pandemic (64 views)
J Clin Med (ISSN: 2077-0383linking, 2077-0383electronic), 2020 Aug 3; 9(8): N/D-N/D.
Impact Factor: 6.78
View Export to BibTeX Export to EndNote
Testino G, Fagoonee S
* Coronavirus disease 2019 outbreak: liver disease a prognostic tool? (97 views)
Panminerva Med (ISSN: 0031-0808linking, 1827-1898electronic), 2020 May 14; N/D: N/D-N/D.
Impact Factor: 3.467
View Export to BibTeX Export to EndNote
D'Andrea A, Radmilovic J, Carbone A, Forni A, Tagliamonte E, Riegler L, Liccardo B, Crescibene F, Sirignano C, Esposito G, Bossone E
* Multimodality imaging in COVID-19 patients: A key role from diagnosis to prognosis (78 views) (PDF 11 views)
World Journal Of Radiology, 2020 May; 21(5): 345-353.
Impact Factor: 0.57
View Export to BibTeX Export to EndNote
Costanzo M, De Giglio MAR, Roviello GN
* SARS-CoV-2: Recent Reports on Antiviral Therapies Based on Lopinavir/Ritonavir, Darunavir/Umifenovir, Hydroxychloroquine, Remdesivir, Favipiravir and other Drugs for the Treatment of the New Coronavirus (298 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2020 Apr 16; 27(27): 4536-4541.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Vincenzi M, Mercurio FA, Leone M
* Protein Interaction Domains and Post-Translational Modifications: Structural Features and Drug Discovery Applications (80 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2020; 27(37): 6306-6355.
Impact Factor: 4.184
View Export to BibTeX Export to EndNote
Vincenzi M, Mercurio FA, Leone M
* Sam Domains in Multiple Diseases (237 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2020; 27(3): 450-476.
Impact Factor: 3.469
View Export to BibTeX Export to EndNote
Balasco N, Barone D, Sandomenico A, Ruggiero A, Doti N, Berisio R, Ruvo M, Vitagliano L
* Structural Versatility of Hepatitis C Virus Proteins: Implications for the Design of Novel Anti-HCV Intervention Strategies (290 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2017 Nov 24; 24(36): 4081-4101.
Impact Factor: 3.469
View Export to BibTeX Export to EndNote
De Rosa L, Romanelli A, D'Andrea LD
* Chemical ligation in Structural Biology in “Chemical Ligation: Tools for Biomolecules Synthesis and Modification” (286 views)
John Wiley & Sons, 2017; N/D: N/D-N/D.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Lanza V, Travaglia A, Malgieri G, Fattorusso R, GrassoG, Di Natale G, Zito V, Arena G, Milardi D, Rizzarelli E
* Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions (279 views) (PDF 172 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2016 Dec 05; 22(49): 17767-17775.
Impact Factor: 5.317
View Export to BibTeX Export to EndNote
Vergara A, Lorber B, Sauter C, Giege R, Zagari A
* Lessons from crystals grown in the Advanced Protein Crystallisation Facility for conventional crystallisation applied to structural biology (369 views)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005; 118(2-3): 102-112.
Impact Factor: 1.925
View Export to BibTeX Export to EndNote
42 Records (41 excluding Abstracts).
Total impact factor: 175.911 (172.218 excluding Abstracts).
Total 5 year impact factor: 141.962 (138.123 excluding Abstracts).
Total impact factor: 175.911 (172.218 excluding Abstracts).
Total 5 year impact factor: 141.962 (138.123 excluding Abstracts).
421 views. Last view on Wednesday 29 March 2023, 2:30:40
ibb.cnr.it
