Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes(593 views) Vitiello G, Falanga A, Galdiero M, Marsh D, Galdiero S, D'Errico G
Department of Chemistry, University of Naples Federico II, Monte Sant'Angelo, 80126, Naples, Italy
CSGI, Consorzio Interuniversitario per Lo Sviluppo Dei Sistemi A Grande Interfase, via della Lastruccia 3, SestoFiorentino, 50019, Florence, Italy
Department of Biological Sciences, Division of Biostructures, University of Naples Federico II, Via Mezzocannone 16, 80134, Naples, Italy
CIRPeB, Centro Interuniversitario di Ricerca sui Peptidi Bioattivi, 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, Napoli, Italy
Max-Planck-Institut für Biophysikalische Chemie, 37077 Göttingen, Germany
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Jensen, M. O., Mouritsen, O. G., Lipids do influence protein function - The hydrophobic matching hypothesis revisited (2004) Biochimica et Biophysica Acta - Biomembranes, 1666 (1-2), pp. 205-226. , DOI 10. 1016/j. bbamem. 2004. 06. 009, PII S0005273604001634, Lipid-Protein Interactions
Chernomordik, L. V., Kozlov, M. M., Mechanics of membrane fusion (2008) Nature Structural and Molecular Biology, 15 (7), pp. 675-683. , DOI 10. 1038/nsmb. 1455, PII NSMB1455
Hurley, J. H., Boura, E., Crlson, L. A., R zycki, B., Membrane budding (2010) Cell, 143, pp. 875-887
Peisajovich, S. G., Shai, Y., Viral fusion proteins: Multiple regions contribute to membrane fusion (2003) Biochimica et Biophysica Acta - Biomembranes, 1614 (1), pp. 122-129. , DOI 10. 1016/S0005-2736 (03) 00170-6
Chowdary, T. K., Cairns, T. M., Atanasiu, D., Cohen, G. H., Eisenberg, R. J., Heldwein, E. E., Crystal structure of the conserved herpes virus fusion regulator complex gH-gL (2010) Nat. Struct. Mol. Biol., 17, pp. 882-888
Cole, N. L., Grose, C., Membrane fusion mediated by herpesvirus glycoproteins: The paradigm of varicella-zoster virus (2003) Reviews in Medical Virology, 13 (4), pp. 207-222. , DOI 10. 1002/rmv. 377
Subramanian, R. P., Geraghty, R. J., Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B (2007) Proceedings of the National Academy of Sciences of the United States of America, 104 (8), pp. 2903-2908. , DOI 10. 1073/pnas. 0608374104
Heldwein, E. E., Lou, H., Bender, F. C., Cohen, G. H., Eisenberg, R. J., Harrison, S. C., Crystal structure of glycoprotein B from herpes simplex virus 1 (2006) Science, 313 (5784), pp. 217-220. , DOI 10. 1126/science. 1126548
Jackson, J. O., Longnecker, R., Reevaluating herpes simplex virus hemifusion (2010) J. Virol., 84, pp. 11814-11821
Harrison, S. C., Viral membrane fusion (2008) Nature Structural and Molecular Biology, 15 (7), pp. 690-698. , DOI 10. 1038/nsmb. 1456, PII NSMB1456
Rama Krishna, Y. V. S., Marsh, D., Spin label ESR and 31P-NMR studies of the cubic and inverted hexagonal phases of dimyristoylphosphatidylcholine/myristic acid (1: 2, mol/mol) mixtures (1990) Biochimica et Biophysica Acta - Biomembranes, 1024 (1), pp. 89-94. , DOI 10. 1016/0005-2736 (90) 90211-6
Struck, D. K., Hoekstra, D., Pagano, R. E., Use of resonance energy transfer to monitor membrane fusion (1981) Biochemistry, 20, pp. 4093-4099
White, S. H., Wimley, W. C., Hydrophobic interactions of peptides with membrane interfaces (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes, 1376 (3), pp. 339-352. , DOI 10. 1016/S0304-4157 (98) 00021-5, PII S0304415798000215
Ladokhin, A. S., White, S. H., Folding of amphipathic -helices on membranes: Energetics of helix formation by melittin (1999) Journal of Molecular Biology, 285 (4), pp. 1363-1369. , DOI 10. 1006/jmbi. 1998. 2346
Sankaram, M. B., Brophy, P. J., Marsh, D., Spin-label ESR studies on the interaction of bovine spinal cord myelin basic protein with dimyristoylphosphatidylglycerol dispersions (1989) Biochemistry, 28 (25), pp. 9685-9691. , DOI 10. 1021/bi00451a022
Sankaram, M. B., De Kruijff, B., Marsh, D., Selectivity of interaction of spin-labelled lipids with peripheral proteins bound to dimyristoylphosphatidylglycerol bilayers, as determined by ESR spectroscopy (1989) Biochimica et Biophysica Acta - Biomembranes, 986 (2), pp. 315-320. , DOI 10. 1016/0005-2736 (89) 90483-5
Meng, F. -G., Zeng, X., Hong, Y. -K., Zhou, H. -M., Dissociation and unfolding of GCN4 leucine zipper in the presence of sodium dodecyl sulfate (2001) Biochimie, 83 (10), pp. 953-956. , DOI 10. 1016/S0300-9084 (01) 01340-2
Veiga, M. P., Goni, F. M., Alonso, A., Marsh, D., Mixed membranes of sphingolipids and glycerolipids as studied by spin-label ESR spectroscopy. A search for domain formation (2000) Biochemistry, 39 (32), pp. 9876-9883. , DOI 10. 1021/bi000678r
Veiga, M. P., Arrondo, J. L. R., Goni, F. M., Alonso, A., Marsh, D., Interaction of cholesterol with sphingomyelin in mixed membranes containing phosphatidylcholine, studied by spin-label ESR and IR spectroscopies. A possible stabilization of gel-phase sphingolipid domains by cholesterol (2001) Biochemistry, 40 (8), pp. 2614-2622. , DOI 10. 1021/bi0019803
Van Genderen, I. L., Brandimarti, R., Torrisi, M. R., Campadelli, G., Van Meer, G., The phospholipid composition of extracellular herpes simplex virions differs from that of host cell nuclei (1994) Virology, 200 (2), pp. 831-836. , DOI 10. 1006/viro. 1994. 1252
Linda, J. P., Xianlin, H., Koong-Nah, C., Richard, W. G., Lipid rafts are enriched in arachidonic acid and plasmenylethanolamine and their composition is independent of caveolin-1 expression: A quantitative electrospray ionization/mass spectrometric analysis (2002) Biochemistry, 41, pp. 2075-2088
Bender, F. C., Whitbeck, J. C., De Leon, M. P., Lou, H., Eisenberg, R. J., Cohen, G. H., Specific association of glycoprotein B with lipid rafts during herpes simplex virus entry (2003) Journal of Virology, 77 (17), pp. 9542-9552. , DOI 10. 1128/JVI. 77. 17. 9542-9552. 2003
Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes
Lipid membranes play a key role in the viral life cycle. Enveloped viruses particularly require a sequence of fusion and fission events between the viral envelope and the target membranes for entry into the cell and egress from it. These processes are controlled by one or more viral glycoproteins that undergo conformational changes favoring the necessary micro- and mesoscopic lipid re-arrangements. Multiple regions from these glycoproteins are thought to interact with the membranes, according to a concerted mechanism, in order to generate the distortion necessary for fusion. In this work, we perform an EPR study on the role played by the membrane composition in tuning the interaction between lipid bilayers and two peptides, gH626-644 and gB632-650, that are highly fusogenic fragments of the gH and gB glycoproteins of herpes simplex virus. Our results show that both peptides interact with lipid bilayers, perturbing the local lipid packing. gH626-644 localizes close to the hydrophilic bilayer surface, while gB632-650 penetrates deeply into the membrane. Chain perturbation by the peptides increases in the presence of charged phospholipids. Finally, cholesterol does not alter the ability of gB632-650 to penetrate deeply in the membrane, whereas it limits penetration of the gH626-644 peptide to the more external layer. The different modes of interaction result in a higher fusogenic ability of gB632-650 towards cholesterol-enriched membranes, as demonstrated by lipid mixing assays. These results suggest that the mechanism of action of the gH and gB glycoproteins is modulated by the properties and composition of the phospholipid bilayer. (C) 2011 Elsevier B.V. All rights reserved.
Lipid composition modulates the interaction of peptides deriving from herpes simplex virus type I glycoproteins B and H with biomembranes
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