Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and(619 views) Galdiero S, Vitiello M, D'Isanto M, Falanga A, Collins C, Raieta K, Pedone C, Browne H, Galdiero M
Journal Of General Virology (ISSN: 0022-1317), 2006 May; 87: 1085-1097.
Keywords: Cell Receptor, Glycoprotein B, Synthetic Peptide, Unclassified Drug, Virus Glycoprotein, Virus Protein, Alpha Helix, Amino Terminal Sequence, Article, Cell Fusion, Cell Membrane, Circular Dichroism, Controlled Study, Gel Permeation Chromatography, Herpes Simplex, Herpes Simplex Virus 1, Human, Human Cell, Inoculation, Membrane Fusion, Nucleotide Repeat, Peptide Analysis, Polyacrylamide Gel Electrophoresis, Prediction, Priority Journal, Protein Domain, Protein Interaction, Virus Infectivity, Virus Inhibition, Virus Transmission, Amino Acid Sequence, Animals, Cercopithecus Aethiops, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Tertiary, Simplexvirus, Vero Cells, Viral Envelope Proteins, Virus Replication, Human Herpesvirus 1,
Affiliations: *** IBB - CNR ***
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Department of Experimental Medicine, II University of Naples, Via De Crecchio 7, 80138 Naples, Italy
Division of Virology, Department of Pathology, University of Cambridge, Cambridge, United Kingdom
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Joshi, S. B., Dutch, R. E., Lamb, R. A., A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41 (1998) Virology, 248, pp. 20-34
Kilby, J. M., Hopkins, S., Venetta, T. M., Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry (1998) Nat Med, 4, pp. 1302-1307. , & 12 other authors
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Malashkevich, V. N., Chan, D. C., Chutkowski, C. T., Kim, P. S., Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: Conserved helical interactions underlie the broad inhibitory activity of gp41 peptides (1998) Proc Natl Acad Sci U S A, 95, pp. 9134-9139
Melikyan, G. B., Markosyan, R. M., Hemmati, H., Delmedico, M. K., Lambert, D. M., Cohen, F. S., Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion (2000) J Cell Biol, 151, pp. 413-423
Mettenleiter, T. C., Brief overview on cellular virus receptors (2002) Virus Res, 82, pp. 3-8
Montgomery, R. I., Warner, M. S., Lum, B. J., Spear, P. G., Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family (1996) Cell, 87, pp. 427-436
Russell, C. J., Jardetzky, T. S., Lamb, R. A., Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion (2001) EMBO, 120, pp. 4024-4034
Spear, P. G., Longnecker, R., Herpesvirus entry: An update (2003) J Virol, 77, pp. 10179-10185
Warner, M. S., Geraghty, R. J., Martinez, W. M., Montgomery, R. I., Whitbeck, J. C., Xu, R., Eisenberg, R. J., Spear, P. G., A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus (1998) Virology, 246, pp. 179-189
Wild, T. F., Buckland, R., Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein (1997) J Gen Virol, 78, pp. 107-111
Wild, C. T., Shugars, D. C., Greenwell, T. K., McDanal, C. B., Matthews, T. J., Peptides corresponding to a predictive -helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection (1994) Proc Natl Acad Sci U S A, 91, pp. 9770-9774
Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and
Human herpesviruses enter cells by fusion of their own membrane with a cellular membrane through the concerted action of multiple viral proteins and cellular receptors. Two conserved viral glycoproteins, gB and gH, are required for herpes simplex virus type 1 (HSV-1)-mediated membrane fusion, but little is known of how these proteins cooperate during entry. Both glycoproteins were shown to contain heptad repeat (HR) sequences predicted to form a-helical coiled coils, and the inhibitory activity against infection of four sets of synthetic peptides corresponding to HR1 and HR2 of gB and gH was tested. The interactions between these HR peptides were also investigated by circular dichroism, native polyacrylamide-gel electrophoresis and size exclusion high-performance liquid chromatography. gH coiled-coil peptides were more effective than gB coiled-coils peptides in inhibiting virus infectivity. The peptides did not impair fusion when added to cells immediately after infection. In contrast, inhibition of infection was observed, albeit to various extents, when peptides were added to virus before or during inoculation. The results of biophysical analyses were indicative of the existence of an interaction between HR1 and HR2 of gH and suggest that the HRs of gB and gH do not interact with each other.
Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and
Petraglia F, Singh AA, Carafa V, Nebbioso A, Conte M, Scisciola L, Valente S, Baldi A, Mandoli A, Petrizzi VB, Ingenito C, De Falco S, Cicatiello V, Apicella I, Janssen-megens EM, Kim B, Yi G, Logie C, Heath S, Ruvo M, Wierenga ATJ, Flicek P, Yaspo ML, Della Valle V, Bernard O, Tomassi S, Novellino E, Feoli A, Sbardella G, Gut I, Vellenga E, Stunnenberg HG, Mai A, Martens JHA, Altucci L * Combined HAT/EZH2 modulation leads to cancer-selective cell death(289 views) Oncotarget (ISSN: 1949-2553electronic, 1949-2553linking), 2018 May 22; 9(39): 25630-25646. Impact Factor:5.008 ViewExport to BibTeXExport to EndNote