Interaction of influenza virus fusion peptide with lipid membranes: Effect of lysolipid

Journal of Membrane Biology

Volumn 211, Issue 3, 2006, Pages 191-200

  Ohki, S ^a   Baker, G A ^b   Page, P M ^c   McCarty, T A ^c   Epand, R M ^d   Bright, F V ^c  

^a UNIVERSITY AT BUFFALO   (United States)

^b OAK RIDGE NATIONAL LABORATORY   (United States)

^c UNIVERSITY AT BUFFALO   (United States)

^d MCMASTER UNIVERSITY   (Canada)

Author keywords

Fluorescence and monolayer studies; Membrane fusion and leakage; Peptide adsorption onto membranes; Viral fusion peptide

Indexed keywords

GLUTAMIC ACID; LIPID; LYSOLIPID; LYSOPHOSPHATIDYLCHOLINE; MUTANT PROTEIN; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE; VIRUS FUSION PROTEIN;

ADSORPTION; AMINO ACID SUBSTITUTION; ARTICLE; CONCENTRATION RESPONSE; CORRELATION COEFFICIENT; FLUORESCENCE SPECTROSCOPY; INFLUENZA VIRUS; LIPID MEMBRANE; LIPID MONOLAYER; LIPID VESICLE; PH; PROTEIN LIPID INTERACTION; SURFACE TENSION;

ADSORPTION; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; LYSOPHOSPHATIDYLCHOLINES; MEMBRANE FUSION; MEMBRANE LIPIDS; ORTHOMYXOVIRIDAE; PEPTIDE FRAGMENTS; PROTEIN BINDING; SURFACE TENSION; UNILAMELLAR LIPOSOMES; VIRAL FUSION PROTEINS;

ORTHOMYXOVIRIDAE;

EID: 33751265496     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-006-0862-z     Document Type: Article

References (34)

1. Bailey, A., Zhukovsky, M., Gliozzi, A., Chernomordik, L.V. 2005. Liposome composition effects on lipid mixing between cells expressing influenza virus hemagglutinin and bound liposomes. Arch. Biochem. Biophys. 439:211-221
2. Baker, G.A., Pandey, S., Bright, F.V. 1999. Multi harmonic Fourier (MHF) Phase-Modulation Fluorescence Spectroscopy with Laser excitation at 257.3nm. Appl. Spectrosc. 53:1475-1479
3. Baljinnyam, B., Schroth-Diez, B., Korte, T., Herrmann, A. 2000. Lysolipids do not inhibit Influenza virus fusion by interaction with hemagglutinin. J. Biol. Chem. 277:20461-20467
4. 2 quenching study. J. Sol-Gel Sci. Tech. 17:83-90
5. Carr, C.M., Kim, P.S. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832
6. Chen, J., Wharton, S.A., Weissenhorn, W., Calder, L.J., Hughson, F.M., Skehel, J.J., Wiley, D.C. 1995. A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation, Proc. Natl. Acad. Sci. USA 92:12205-12209
7. Chernomodik, L.V., Vogel, S.S., Sokoloff, A., Onaran, H.O., Leikin, E.A., Zimmerberg, J. 1993. Lysolipids reversibly inhibit Ca(2+)-, GTP- and pH-dependent fusion of biological membranes. FEBS Lett. 318:71-76
8. Clague, M.J., Knutson, J.R., Blumenthal, R., Herrmann, A. 1991. Interaction of influenza hemagglutinin amino-terminal peptide with phospholipid vesicles: A fluorescence study. Biochemistry 30:5491-5497
9. Colotto, A., Epand, R.M. 1997. Structural study of the relationship between the rate of membrane fusion and the ability of the fusion peptide of Influenza virus to perturb bilayers. Biochemistry. 36:7644-7651
10. Doms, R.W., Helenius, A., White, J. 1985. Membrane fusion activity of the influenza virus hemagglutinin. J. Biol. Chem. 260:2973-2981
11. Epand, R.M. 2003. Fusion peptides and the mechanism of viral fusion. Biochim. Biophys. Acta 1614:116-121
12. Epand, R.F., Macosko, J.C., Russell, C.J., Shin, Y.-K., Epand, R.M. 1999. The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion. J. Mol. Biol. 286:489-503
13. Epand, R.M., Epand, R.F., Martin, I., Ruysschaert, J-M. 2001. Membrane interactions of mutated forms of the Influenza fusion peptide. Biochemistry 40:8800-8807
14. Ellens, H., Bentz, J., Szoka, F.C. 1984. pH-induced destabilization of phosphatidylethanolamine-containing liposomes: Role of bilayer contact. Biochemistry 23:1532-1538
15. Gething, M.J., Doms, R.W., York, D., White, J. 1986. Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemaggulutinin of influenza virus. J. Cell Biol. 102:11-23
16. Gunther-Ausborn, S., Praetor, A., Stegmann, T. 1995. Inhibition of Influenza-induced membrane fusion by lysophosphatidylcholine. J. Biol.Chem. 270:29279-29285
17. Hoekstra, D., Duzgunes, N. 1993. Lipid mixing assays to determine fusion in liposomes systems. Methods Enzym. 220:15-32
18. Korte, T., Epand, R.F., Epand, R.M., Blumenthal, R. 2001. Role of the Glu residues of the influenza hemagglutinin fusion peptide in the pH dependence of fusion activity. Virology 289:353-361
19. 2. J. Biol. Chem. 262:6500-6505
20. Maeda, T., Kawasaki, K., Ohnishi, S. 1981. Interaction of influenza virus hemagglutinin with target membranes lipid is a key step in virus-induced hemolysis and fusion at pH 5.2. Proc. Natl. Acad. Sci. USA 78:4133-4137
21. Martin, I., Dubois, M.C., Defrrise-Quertain, F., Saermark, T., Burny, A., Brasseur, R., Ruysschaert, J.M. 1994. Correlation between fusogenicity of synthetic modified peptide corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study. J. Virol. 68:1139-1148
22. Martin, I., Ruysschaert, J.M. 1995. Lysophosphatidylcholine inhibits vesicle fusion induced by the NH2-terminal extremity of SIV/IV fusogenic proteins. Biochim. Biophys. Acta 1240:95-100
23. Ohki, S., Duzgunes, N. 1979. Divalent cation-induced interaction of phospholipid vesicle and monolayer membranes. Biochim. Biophys. Acta 552:438-449
24. Ohki, S., Arnold, K. 2000. A mechanism for ion-induced lipid vesicle fusion. Colloid and Surfaces B: Biointerfaces 18:83-97
25. Ohki, S., Arnold, K. 2003. Surface dielectric constant of lipid vesicles. Methods. Enzym. 367:255-272
26. Pecheur, E. I., Martin, I., Bienvenue, A., Ruysschaert, J. M., Hoekstra, D. 2000. Protein-induced fusion can be modulated by target membrane lipids through a structural switch at the level of the fusion peptide. J. Biol. Chem. 275:3936-3942
27. Razinkov, V., Melikyan, G.B., Epand, R.M., Epand, R.F., Cohen, F.S. 1998. Effects of spontaneous bilayer curvature on Influenza virus-mediated fusion pores. J. Gen. Physiol. 112:409-422
28. Ruggiero, A.J., Todd, D.C., Fleming, G.R. 1990. Subpicosecond fluorescence anisotropy studies of tryptophan in water. J. Am. Chem. Soc. 112:1003-1014
29. Skehel, J.J., Bayley, P.M., Brown, E.B., Martin, S.R., Waterfield, M.D., White, J.M., Wilson, I.J., Wiley, D.C. 1982. Changes in the conformation of influenza virus hemagglutinin at the pH optimum of virus-mediated membrane fusion. Proc. Natl. Acad. Sci. USA 79:968-972
30. Stegmann, T., Hoekstra, D., Scherphof, G., Wilschut, J. 1986. Fusion activity of influenza virus. J. Biol. Chem. 261:10966-10969
31. Stegmann, T., Deffino, J. M., Richards, F.M., Helenius, A. 199x. The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior fusion. J. Biol. Chem. 266:18404-18410
32. Trivedi, V. D., Yu, C., Veeramuthu, B., Francis, S., Chang, D. K. 2000. Fusion induced aggregation of model vesicles studied by dynamic and static light scattering. Chem. Phys. Lipids 107:99-106
33. Valeur, B., Webber, G. 1977. Resolution of the fluorescence excitation spectrum of indole into the 1La and 1Lb excitation bands. Photochem. Photobiol. 25:441-444
34. Wharton, S.A., Martin, S.R., Ruigrok, R.W., Skehel, J.J., Wiley, D.C. 1988. Membrane fusion by peptide analogues of influenza virus haemagglutinin. J. Gen. Virol. 69:1847-1857