The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein (471 views)
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2010 May 28; 285(22): 17123-17136.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.328, 5-year impact factor: 5.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952758845&partnerID=40&md5=ca6d9ec1c38ab3d8e6377c48f09ec5ce
Keywords: Different Domains, Ectodomain, Helical Domains, Herpes Simplex Virus Type 1, Heterodimers, Histidine Residues, Membrane Fusion, Model Membranes, N-Terminals, Non-Covalent Interaction, Synthetic Peptide, Amino Acids, Cell Membranes, Magnetic Domains, Nuclear Magnetic Resonance, Organic Acids, Phosphatases, Glycoproteins, Unclassified Drug, Virus Glycoprotein, Alpha Helix, Amino Terminal Sequence, Article, Controlled Study, Nonhuman, Priority Journal, Protein Domain, Acrylamide, Algorithms, Herpesvirus 1, Kinetics, Lipids, Liposomes, Magnetic Resonance Spectroscopy, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Surface Plasmon Resonance, Tryptophan, Viral Envelope Proteins, Human Herpesvirus 1,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy. sgaldier@unina.it
Dept. of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy
Dept. of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, Napoli 80134, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Napoli 80134, Italy
Istituto di Biostrutture e Bioimmagini-Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, Napoli 80134, Italy
Department of Environmental Sciences, II University of Naples, via Vivaldi 43, Caserta 81100, Italy
References:
White, J.M., Delos, S.E., Brecher, M., Schornberg, K., (2008) Crit. Rev. Biochem. Mol. Biol., 43, pp. 189-21
Harrison, S.C., (2008) Nat. Struct. Mol. Biol., 15, pp. 690-698
Weissenhorn, W., Hinz, A., Gaudin, Y., (2007) FEBS Lett., 581, pp. 2150-2155
Kielian, M., Rey, F.A., (2006) Nat. Rev. Microbiol., 4, pp. 67-76
Brasseur, R., Pillot, T., Lins, L., Vandekerckhove, J., Rosseneu, M., (1997) Trends Biochem. Sci., 22, pp. 167-171
Durell, S.R., Martin, I., Ruysschaert, J.M., Shai, Y., Blumenthal, R., (1997) Mol. Membr. Biol., 14, pp. 97-112
Zhu, N.L., Cannon, P.M., Chen, D., Anderson, W.F., (1998) J. Virol., 72, pp. 1632-1639
Madu, I.G., Roth, S.L., Belouzard, S., Whittaker, G.R., (2009) J. Virol., 83, pp. 7411-7421
Hannah, B.P., Heldwein, E.E., Bender, F.C., Cohen, G.H., Eisenberg, R.J., (2007) J. Virol., 81, pp. 4858-4865
Shai, Y., (2000) Biosci. Rep., 20, pp. 535-555
Tamm, L.K., Han, X., (2000) Biosci. Rep., 20, pp. 501-518
Skehel, J.J., Cross, K., Steinhauer, D., Wiley, D.C., (2001) Biochem. Soc. Trans., 29, pp. 623-626
Guillén, J., Kinnunen, P.K., Villalaín, J., (2008) Biochim. Biophys. Acta, 1778, pp. 2765-2774
Galdiero, S., Falanga, A., Vitiello, M., Browne, H., Pedone, C., Galdiero, M., (2005) J. Biol. Chem., 280, pp. 28632-28643
Spear, P.G., Longnecker, R., (2003) J. Virol., 77, pp. 10179-10185
Heldwein, E.E., Krummenacher, C., (2008) Cell. Mol. Life Sci., 65, pp. 1653-1668
Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Galdiero, M., (2006) J. Gen. Virol., 87, pp. 1085-1097
Cai, W.H., Gu, B., Person, S., (1988) J. Virol., 62, pp. 2596-2604
Forrester, A., Farrell, H., Wilkinson, G., Kaye, J., Davis-Poynter, N., Minson, T., (1992) J. Virol., 66, pp. 341-348
Subramanian, R.P., Geraghty, R.J., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, pp. 2903-2908
Atanasiu, D., Whitbeck, J.C., Cairns, T.M., Reilly, B., Cohen, G.H., Eisenberg, R.J., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, pp. 18718-18723
Avitabile, E., Forghieri, C., Campadelli-Fiume, G., (2007) J. Virol., 81, pp. 11532-11537
Heldwein, E.E., Lou, H., Bender, F.C., Cohen, G.H., Eisenberg, R.J., Harrison, S.C., (2006) Science, 313, pp. 217-220
Roche, S., Bressanelli, S., Rey, F.A., Gaudin, Y., (2006) Science, 313, pp. 187-191
Gage, P.J., Levine, M., Glorioso, J.C., (1993) J. Virol., 67, pp. 2191-2201
Backovic, M., Jardetzky, T.S., (2009) Curr. Opin. Struct. Biol., 19, pp. 189-196
Kielian, M., (2006) Virology, 344, pp. 38-47
Schibli, D.J., Weissenhorn, W., (2004) Mol. Membr. Biol., 21, pp. 361-371
Gianni, T., Martelli, P.L., Casadio, R., Campadelli-Fiume, G., (2005) J. Virol., 79, pp. 2931-2940
Cairns, T.M., Landsburg, D.J., Whitbeck, J.C., Eisenberg, R.J., Cohen, G.H., (2005) Virology, 332, pp. 550-562
Galdiero, M., Whiteley, A., Bruun, B., Bell, S., Minson, T., Browne, H., (1997) J. Virol., 71, pp. 2163-2170
Harman, A., Browne, H., Minson, T., (2002) J. Virol., 76, pp. 10708-10716
Wilson, D.W., Davis-Poynter, N., Minson, A.C., (1994) J. Virol., 68, pp. 6985-6993
Gianni, T., Menotti, L., Campadelli-Fiume, G., (2005) J. Virol., 79, pp. 7042-7049
Lopper, M., Compton, T., (2004) J. Virol., 78, pp. 8333-8341
Fiske, C.H., Subbarow, Y., (1925) J. Biol. Chem., 66, pp. 374-389
Schwarz, G., Stankowski, S., Rizzo, V., (1986) Biochim. Biophys. Acta, 861, pp. 141-151
Beschiaschvili, G., Seelig, J., (1990) Biochemistry, 29, pp. 52-58
De Kroon, A.I., Soekarjo, M.W., De Gier, J., De Kruijff, B., (1990) Biochemistry, 29, pp. 8229-8240
Eftink, M.R., Ghiron, C.A., (1976) J. Phys. Chem., 80, pp. 486-493
Kalb, E., Frey, S., Tamm, L.K., (1992) Biochim. Biophys. Acta, 1103, pp. 307-316
Morton, T.A., Myszka, D.G., Chaiken, I.M., (1995) Anal. Biochem., 227, pp. 176-185
Shai, Y., (1999) Biochim. Biophys. Acta, 1462, pp. 55-70
Mozsolits, H., Wirth, H.J., Werkmeister, J., Aguilar, M.I., (2001) Biochim. Biophys. Acta, 1512, pp. 64-76
Cavanagh, J., Fairbrother, W., Palmer III, A.G., Skelton, N.J., (1996) Protein NMR Spectroscopy, Principles, and Practice, , Academic Press, Inc., San Diego, CA
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. A, 112, pp. 275-279
Bartels, C., Xia, T., Billeter, M., Guntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, pp. 1-10
Herrmann, T., Güntert, P., Wüthrich, K., (2002) J. Mol. Biol., 319, pp. 209-227
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graph., 14, pp. 51-55
Lüneberg, J., Martin, I., Nüssler, F., Ruysschaert, J.M., Herrmann, A., (1995) J. Biol. Chem., 270, pp. 27606-27614
Galdiero, S., Galdiero, M., Pedone, C., Falanga, A., Vitiello, M., (2009), 12/11/ U. S. Patent Provisional 61/285,619Yau, W.M., Wimley, W.C., Gawrisch, K., White, S.H., (1998) Biochemistry, 37, pp. 14713-14718
Habermann, E., Jentsch, J., (1967) Hoppe-Seyler's Z. Physiol. Chem., 348, pp. 37-50
Rafalski, M., Lear, J.D., Degrado, W.F., (1990) Biochemistry, 29, pp. 7917-7922
Papo, N., Shai, Y., (2003) Biochemistry, 42, pp. 458-466
DeGrado, W.F., Lear, J.D., (1990) Biopolymers, 29, pp. 205-213
Parente, R.A., Nadasdi, L., Subbarao, N.K., Szoka Jr., F.C., (1990) Biochemistry, 29, pp. 8713-8719
Gordon, L.M., Curtain, C.C., Zhong, Y.C., Kirkpatrick, A., Mobley, P.W., Waring, A.J., (1992) Biochim. Biophys. Acta, 1139, pp. 257-274
Wishart, D.S., Case, D.A., (2001) Methods Enzymol., 338, pp. 3-34
Vitiello, M., Galdiero, M., Galdiero, M., (2009) Protein Pept. Lett., 16, pp. 786-793
Krishnan, A., Verma, S.K., Mani, P., Gupta, R., Kundu, S., Sarkar, D.P., (2009) J. Virol., 83, pp. 1727-1741
Chanel-Vos, C., Kielian, M., (2004) J. Virol., 78, pp. 13543-13552
Freed, E.O., Myers, D.J., (1992) J. Virol., 66, pp. 5472-5478
Steinhauer, D.A., Wharton, S.A., Skehel, J.J., Wiley, D.C., (1995) J. Virol., 69, pp. 6643-6651
White, J. M., Delos, S. E., Brecher, M., Schornberg, K., (2008) Crit. Rev. Biochem. Mol. Biol., 43, pp. 189-21
Harrison, S. C., (2008) Nat. Struct. Mol. Biol., 15, pp. 690-698
Durell, S. R., Martin, I., Ruysschaert, J. M., Shai, Y., Blumenthal, R., (1997) Mol. Membr. Biol., 14, pp. 97-112
Zhu, N. L., Cannon, P. M., Chen, D., Anderson, W. F., (1998) J. Virol., 72, pp. 1632-1639
Madu, I. G., Roth, S. L., Belouzard, S., Whittaker, G. R., (2009) J. Virol., 83, pp. 7411-7421
Hannah, B. P., Heldwein, E. E., Bender, F. C., Cohen, G. H., Eisenberg, R. J., (2007) J. Virol., 81, pp. 4858-4865
Tamm, L. K., Han, X., (2000) Biosci. Rep., 20, pp. 501-518
Skehel, J. J., Cross, K., Steinhauer, D., Wiley, D. C., (2001) Biochem. Soc. Trans., 29, pp. 623-626
Guill n, J., Kinnunen, P. K., Villala n, J., (2008) Biochim. Biophys. Acta, 1778, pp. 2765-2774
Spear, P. G., Longnecker, R., (2003) J. Virol., 77, pp. 10179-10185
Heldwein, E. E., Krummenacher, C., (2008) Cell. Mol. Life Sci., 65, pp. 1653-1668
Cai, W. H., Gu, B., Person, S., (1988) J. Virol., 62, pp. 2596-2604
Subramanian, R. P., Geraghty, R. J., (2007) Proc. Natl. Acad. Sci. U. S. A., 104, pp. 2903-2908
Heldwein, E. E., Lou, H., Bender, F. C., Cohen, G. H., Eisenberg, R. J., Harrison, S. C., (2006) Science, 313, pp. 217-220
Gage, P. J., Levine, M., Glorioso, J. C., (1993) J. Virol., 67, pp. 2191-2201
Schibli, D. J., Weissenhorn, W., (2004) Mol. Membr. Biol., 21, pp. 361-371
Cairns, T. M., Landsburg, D. J., Whitbeck, J. C., Eisenberg, R. J., Cohen, G. H., (2005) Virology, 332, pp. 550-562
Wilson, D. W., Davis-Poynter, N., Minson, A. C., (1994) J. Virol., 68, pp. 6985-6993
Fiske, C. H., Subbarow, Y., (1925) J. Biol. Chem., 66, pp. 374-389
De Kroon, A. I., Soekarjo, M. W., De Gier, J., De Kruijff, B., (1990) Biochemistry, 29, pp. 8229-8240
Eftink, M. R., Ghiron, C. A., (1976) J. Phys. Chem., 80, pp. 486-493
Morton, T. A., Myszka, D. G., Chaiken, I. M., (1995) Anal. Biochem., 227, pp. 176-185
Hwang, T. L., Shaka, A. J., (1995) J. Magn. Reson. A, 112, pp. 275-279
Herrmann, T., G ntert, P., W thrich, K., (2002) J. Mol. Biol., 319, pp. 209-227
L neberg, J., Martin, I., N ssler, F., Ruysschaert, J. M., Herrmann, A., (1995) J. Biol. Chem., 270, pp. 27606-27614
DeGrado, W. F., Lear, J. D., (1990) Biopolymers, 29, pp. 205-213
Parente, R. A., Nadasdi, L., Subbarao, N. K., Szoka Jr., F. C., (1990) Biochemistry, 29, pp. 8713-8719
Gordon, L. M., Curtain, C. C., Zhong, Y. C., Kirkpatrick, A., Mobley, P. W., Waring, A. J., (1992) Biochim. Biophys. Acta, 1139, pp. 257-274
Wishart, D. S., Case, D. A., (2001) Methods Enzymol., 338, pp. 3-34
Freed, E. O., Myers, D. J., (1992) J. Virol., 66, pp. 5472-5478
Steinhauer, D. A., Wharton, S. A., Skehel, J. J., Wiley, D. C., (1995) J. Virol., 69, pp. 6643-6651
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2010 May 28; 285(22): 17123-17136.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.328, 5-year impact factor: 5.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952758845&partnerID=40&md5=ca6d9ec1c38ab3d8e6377c48f09ec5ce
Keywords: Different Domains, Ectodomain, Helical Domains, Herpes Simplex Virus Type 1, Heterodimers, Histidine Residues, Membrane Fusion, Model Membranes, N-Terminals, Non-Covalent Interaction, Synthetic Peptide, Amino Acids, Cell Membranes, Magnetic Domains, Nuclear Magnetic Resonance, Organic Acids, Phosphatases, Glycoproteins, Unclassified Drug, Virus Glycoprotein, Alpha Helix, Amino Terminal Sequence, Article, Controlled Study, Nonhuman, Priority Journal, Protein Domain, Acrylamide, Algorithms, Herpesvirus 1, Kinetics, Lipids, Liposomes, Magnetic Resonance Spectroscopy, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Surface Plasmon Resonance, Tryptophan, Viral Envelope Proteins, Human Herpesvirus 1,
Affiliations:
*** IBB - CNR ***
Department of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy. sgaldier@unina.it
Dept. of Experimental Medicine, II University of Naples, Via De Crecchio 7, Napoli 80138, Italy
Dept. of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, Napoli 80134, Italy
Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, University of Naples Federico II, Napoli 80134, Italy
Istituto di Biostrutture e Bioimmagini-Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, Napoli 80134, Italy
Department of Environmental Sciences, II University of Naples, via Vivaldi 43, Caserta 81100, Italy
References:
White, J.M., Delos, S.E., Brecher, M., Schornberg, K., (2008) Crit. Rev. Biochem. Mol. Biol., 43, pp. 189-21
Harrison, S.C., (2008) Nat. Struct. Mol. Biol., 15, pp. 690-698
Weissenhorn, W., Hinz, A., Gaudin, Y., (2007) FEBS Lett., 581, pp. 2150-2155
Kielian, M., Rey, F.A., (2006) Nat. Rev. Microbiol., 4, pp. 67-76
Brasseur, R., Pillot, T., Lins, L., Vandekerckhove, J., Rosseneu, M., (1997) Trends Biochem. Sci., 22, pp. 167-171
Durell, S.R., Martin, I., Ruysschaert, J.M., Shai, Y., Blumenthal, R., (1997) Mol. Membr. Biol., 14, pp. 97-112
Zhu, N.L., Cannon, P.M., Chen, D., Anderson, W.F., (1998) J. Virol., 72, pp. 1632-1639
Madu, I.G., Roth, S.L., Belouzard, S., Whittaker, G.R., (2009) J. Virol., 83, pp. 7411-7421
Hannah, B.P., Heldwein, E.E., Bender, F.C., Cohen, G.H., Eisenberg, R.J., (2007) J. Virol., 81, pp. 4858-4865
Shai, Y., (2000) Biosci. Rep., 20, pp. 535-555
Tamm, L.K., Han, X., (2000) Biosci. Rep., 20, pp. 501-518
Skehel, J.J., Cross, K., Steinhauer, D., Wiley, D.C., (2001) Biochem. Soc. Trans., 29, pp. 623-626
Guillén, J., Kinnunen, P.K., Villalaín, J., (2008) Biochim. Biophys. Acta, 1778, pp. 2765-2774
Galdiero, S., Falanga, A., Vitiello, M., Browne, H., Pedone, C., Galdiero, M., (2005) J. Biol. Chem., 280, pp. 28632-28643
Spear, P.G., Longnecker, R., (2003) J. Virol., 77, pp. 10179-10185
Heldwein, E.E., Krummenacher, C., (2008) Cell. Mol. Life Sci., 65, pp. 1653-1668
Galdiero, S., Vitiello, M., D'Isanto, M., Falanga, A., Collins, C., Raieta, K., Pedone, C., Galdiero, M., (2006) J. Gen. Virol., 87, pp. 1085-1097
Cai, W.H., Gu, B., Person, S., (1988) J. Virol., 62, pp. 2596-2604
Forrester, A., Farrell, H., Wilkinson, G., Kaye, J., Davis-Poynter, N., Minson, T., (1992) J. Virol., 66, pp. 341-348
Subramanian, R.P., Geraghty, R.J., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, pp. 2903-2908
Atanasiu, D., Whitbeck, J.C., Cairns, T.M., Reilly, B., Cohen, G.H., Eisenberg, R.J., (2007) Proc. Natl. Acad. Sci. U.S.A., 104, pp. 18718-18723
Avitabile, E., Forghieri, C., Campadelli-Fiume, G., (2007) J. Virol., 81, pp. 11532-11537
Heldwein, E.E., Lou, H., Bender, F.C., Cohen, G.H., Eisenberg, R.J., Harrison, S.C., (2006) Science, 313, pp. 217-220
Roche, S., Bressanelli, S., Rey, F.A., Gaudin, Y., (2006) Science, 313, pp. 187-191
Gage, P.J., Levine, M., Glorioso, J.C., (1993) J. Virol., 67, pp. 2191-2201
Backovic, M., Jardetzky, T.S., (2009) Curr. Opin. Struct. Biol., 19, pp. 189-196
Kielian, M., (2006) Virology, 344, pp. 38-47
Schibli, D.J., Weissenhorn, W., (2004) Mol. Membr. Biol., 21, pp. 361-371
Gianni, T., Martelli, P.L., Casadio, R., Campadelli-Fiume, G., (2005) J. Virol., 79, pp. 2931-2940
Cairns, T.M., Landsburg, D.J., Whitbeck, J.C., Eisenberg, R.J., Cohen, G.H., (2005) Virology, 332, pp. 550-562
Galdiero, M., Whiteley, A., Bruun, B., Bell, S., Minson, T., Browne, H., (1997) J. Virol., 71, pp. 2163-2170
Harman, A., Browne, H., Minson, T., (2002) J. Virol., 76, pp. 10708-10716
Wilson, D.W., Davis-Poynter, N., Minson, A.C., (1994) J. Virol., 68, pp. 6985-6993
Gianni, T., Menotti, L., Campadelli-Fiume, G., (2005) J. Virol., 79, pp. 7042-7049
Lopper, M., Compton, T., (2004) J. Virol., 78, pp. 8333-8341
Fiske, C.H., Subbarow, Y., (1925) J. Biol. Chem., 66, pp. 374-389
Schwarz, G., Stankowski, S., Rizzo, V., (1986) Biochim. Biophys. Acta, 861, pp. 141-151
Beschiaschvili, G., Seelig, J., (1990) Biochemistry, 29, pp. 52-58
De Kroon, A.I., Soekarjo, M.W., De Gier, J., De Kruijff, B., (1990) Biochemistry, 29, pp. 8229-8240
Eftink, M.R., Ghiron, C.A., (1976) J. Phys. Chem., 80, pp. 486-493
Kalb, E., Frey, S., Tamm, L.K., (1992) Biochim. Biophys. Acta, 1103, pp. 307-316
Morton, T.A., Myszka, D.G., Chaiken, I.M., (1995) Anal. Biochem., 227, pp. 176-185
Shai, Y., (1999) Biochim. Biophys. Acta, 1462, pp. 55-70
Mozsolits, H., Wirth, H.J., Werkmeister, J., Aguilar, M.I., (2001) Biochim. Biophys. Acta, 1512, pp. 64-76
Cavanagh, J., Fairbrother, W., Palmer III, A.G., Skelton, N.J., (1996) Protein NMR Spectroscopy, Principles, and Practice, , Academic Press, Inc., San Diego, CA
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. A, 112, pp. 275-279
Bartels, C., Xia, T., Billeter, M., Guntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, pp. 1-10
Herrmann, T., Güntert, P., Wüthrich, K., (2002) J. Mol. Biol., 319, pp. 209-227
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graph., 14, pp. 51-55
Lüneberg, J., Martin, I., Nüssler, F., Ruysschaert, J.M., Herrmann, A., (1995) J. Biol. Chem., 270, pp. 27606-27614
Galdiero, S., Galdiero, M., Pedone, C., Falanga, A., Vitiello, M., (2009), 12/11/ U. S. Patent Provisional 61/285,619Yau, W.M., Wimley, W.C., Gawrisch, K., White, S.H., (1998) Biochemistry, 37, pp. 14713-14718
Habermann, E., Jentsch, J., (1967) Hoppe-Seyler's Z. Physiol. Chem., 348, pp. 37-50
Rafalski, M., Lear, J.D., Degrado, W.F., (1990) Biochemistry, 29, pp. 7917-7922
Papo, N., Shai, Y., (2003) Biochemistry, 42, pp. 458-466
DeGrado, W.F., Lear, J.D., (1990) Biopolymers, 29, pp. 205-213
Parente, R.A., Nadasdi, L., Subbarao, N.K., Szoka Jr., F.C., (1990) Biochemistry, 29, pp. 8713-8719
Gordon, L.M., Curtain, C.C., Zhong, Y.C., Kirkpatrick, A., Mobley, P.W., Waring, A.J., (1992) Biochim. Biophys. Acta, 1139, pp. 257-274
Wishart, D.S., Case, D.A., (2001) Methods Enzymol., 338, pp. 3-34
Vitiello, M., Galdiero, M., Galdiero, M., (2009) Protein Pept. Lett., 16, pp. 786-793
Krishnan, A., Verma, S.K., Mani, P., Gupta, R., Kundu, S., Sarkar, D.P., (2009) J. Virol., 83, pp. 1727-1741
Chanel-Vos, C., Kielian, M., (2004) J. Virol., 78, pp. 13543-13552
Freed, E.O., Myers, D.J., (1992) J. Virol., 66, pp. 5472-5478
Steinhauer, D.A., Wharton, S.A., Skehel, J.J., Wiley, D.C., (1995) J. Virol., 69, pp. 6643-6651
White, J. M., Delos, S. E., Brecher, M., Schornberg, K., (2008) Crit. Rev. Biochem. Mol. Biol., 43, pp. 189-21
Harrison, S. C., (2008) Nat. Struct. Mol. Biol., 15, pp. 690-698
Durell, S. R., Martin, I., Ruysschaert, J. M., Shai, Y., Blumenthal, R., (1997) Mol. Membr. Biol., 14, pp. 97-112
Zhu, N. L., Cannon, P. M., Chen, D., Anderson, W. F., (1998) J. Virol., 72, pp. 1632-1639
Madu, I. G., Roth, S. L., Belouzard, S., Whittaker, G. R., (2009) J. Virol., 83, pp. 7411-7421
Hannah, B. P., Heldwein, E. E., Bender, F. C., Cohen, G. H., Eisenberg, R. J., (2007) J. Virol., 81, pp. 4858-4865
Tamm, L. K., Han, X., (2000) Biosci. Rep., 20, pp. 501-518
Skehel, J. J., Cross, K., Steinhauer, D., Wiley, D. C., (2001) Biochem. Soc. Trans., 29, pp. 623-626
Guill n, J., Kinnunen, P. K., Villala n, J., (2008) Biochim. Biophys. Acta, 1778, pp. 2765-2774
Spear, P. G., Longnecker, R., (2003) J. Virol., 77, pp. 10179-10185
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The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein
Herpes simplex virus type 1 (HSV-1)-induced membrane fusion remains one of the most elusive mechanisms to be deciphered in viral entry. The structure resolution of glycoprotein gB has revealed the presence of fusogenic domains in this protein and pointed out the key role of gB in the entry mechanism of HSV-1. A second putative fusogenic glycoprotein is represented by the heterodimer comprising the membrane-anchored glycoprotein H (gH) and the small secreted glycoprotein L, which remains on the viral envelope in virtue of its non-covalent interaction with gH. Different domains scattered on the ectodomain of HSV-1 gH have been demonstrated to display membranotropic characteristics. The segment from amino acid 626 to 644 represents the most fusogenic region identified by studies with synthetic peptides and model membranes. Herein we have identified the minimal fusogenic sequence present on gH. An enlongation at the N terminus of a single histidine (His) has proved to profoundly increase the fusogenic activity of the original sequence. Nuclear magnetic resonance (NMR) studies have shown that the addition of the N-terminal His contributes to the formation and stabilization of an alpha-helical domain with high fusion propensity.
Herpes simplex virus type 1 (HSV-1)-induced membrane fusion remains one of the most elusive mechanisms to be deciphered in viral entry. The structure resolution of glycoprotein gB has revealed the presence of fusogenic domains in this protein and pointed out the key role of gB in the entry mechanism of HSV-1. A second putative fusogenic glycoprotein is represented by the heterodimer comprising the membrane-anchored glycoprotein H (gH) and the small secreted glycoprotein L, which remains on the viral envelope in virtue of its non-covalent interaction with gH. Different domains scattered on the ectodomain of HSV-1 gH have been demonstrated to display membranotropic characteristics. The segment from amino acid 626 to 644 represents the most fusogenic region identified by studies with synthetic peptides and model membranes. Herein we have identified the minimal fusogenic sequence present on gH. An enlongation at the N terminus of a single histidine (His) has proved to profoundly increase the fusogenic activity of the original sequence. Nuclear magnetic resonance (NMR) studies have shown that the addition of the N-terminal His contributes to the formation and stabilization of an alpha-helical domain with high fusion propensity.
The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein
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The presence of a single N-terminal histidine residue enhances the fusogenic properties of a Membranotropic peptide derived from herpes simplex virus type 1 glycoprotein
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* Conformational modifications of gB from herpes simplex virus type 1 analyzed by synthetic peptides (594 views)
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Impact Factor: 5.48
View Export to BibTeX Export to EndNote
Galdiero S, Russo L, Falanga A, Cantisani M, Vitiello M, Fattorusso R, Malgieri G, Galdiero M, Isernia C
* Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System (368 views)
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Impact Factor: 3.377
View Export to BibTeX Export to EndNote
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Impact Factor: 6.692
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Raiola L, Fattorusso R, Browne H, Pedone C, Isernia C, Galdiero M
* Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein (545 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 31; 283(44): 29993-30009.
Impact Factor: 5.52
View Export to BibTeX Export to EndNote
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Impact Factor: 2.565
View Export to BibTeX Export to EndNote
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Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 25; 8(8): 885-895.
Impact Factor: 3.446
View Export to BibTeX Export to EndNote
Galdiero S, Vitiello M, D'Isanto M, Falanga A, Collins C, Raieta K, Pedone C, Browne H, Galdiero M
* Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and (618 views)
Journal Of General Virology (ISSN: 0022-1317), 2006 May; 87: 1085-1097.
Impact Factor: 3.11
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Browne H, Pedone C, Galdiero M
* Fusogenic domains in herpes simplex virus type 1 glycoprotein (590 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Sep 5; 280(31): 28632-28643.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Galdiero S, Vitiello M, D'Isanto M, Di Niola E, Peluso L, Raieta K, Pedone C, Galdiero M, Benedetti E
* Induction of signaling pathways by herpes simplex virus type 1 through glycoprotein H peptides (589 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004; 76(6): 494-502.
Impact Factor: 2.863
View Export to BibTeX Export to EndNote
11 Records (11 excluding Abstracts).
Total impact factor: 45.262 (45.262 excluding Abstracts).
Total 5 year impact factor: 45.593 (45.593 excluding Abstracts).
Total impact factor: 45.262 (45.262 excluding Abstracts).
Total 5 year impact factor: 45.593 (45.593 excluding Abstracts).
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