Interaction between dengue virus fusion peptide and lipid bilayers depends on peptide clustering

References

• Lindenbach BD, Rice CM. Flaviviridae: The viruses and their replication. Fields’ virology4th ed, BN Fields, PM Howley, DE Griffin, RA Lamb, MA Martin, B Roizman, SE Straus, DM Knipe. Lippincott Williams & Wilkins, Philadelphia 2001; 991–1041
   Google Scholar
• Crill WD, Roehrig JT. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J Virol 2001; 75: 7769–7773
   PubMed Web of Science ®Google Scholar
• Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, Lenches E, Jones CT, Mukhopadhyay S, Chipman PR, Strauss EG, Baker TS, Strauss JH. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell 2002; 108: 717–725
   PubMed Web of Science ®Google Scholar
• Modis Y, Ogata S, Clements D, Harrison SC. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc Natl Acad Sci USA 2003; 100: 6986–6991
   PubMed Web of Science ®Google Scholar
• Modis Y, Ogata S, Clements D, Harrison SC. Structure of the dengue virus envelope protein after membrane fusion. Nature 2004; 427: 313–319
   PubMed Web of Science ®Google Scholar
• Wieprecht T, Beyermann M, Seelig J. Thermodynamics of the coil-alpha-helix transition of amphipathic peptides in a membrane environment: the role of vesicle curvature. Biophys Chem 2002; 96: 191–201
   PubMed Web of Science ®Google Scholar
• Mayer LD, Hope MJ, Cullis PR. Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim Biophys Acta 1986; 858: 161–168
   PubMed Web of Science ®Google Scholar
• Lakowicz JR, 1999. Principles of fluorescence spectroscopy. 2nd ed. New York: Kluwer Academic/Plenum. 725 pp.
   Google Scholar
• Santos NC, Prieto M, Castanho MA. Quantifying molecular partition into model systems of biomembranes: an emphasis on optical spectroscopic methods. Biochim Biophys Acta 2003; 1612: 123–135
   PubMedGoogle Scholar
• Melo MN, Castanho MARB. Omiganan interaction with bacterial membranes and cell wall models. Assigning a biological role to saturation. Biochim Biophys Acta 2007; 1768: 1277–1290
   PubMedGoogle Scholar
• Chiu SW, Jakobsson E, Subramaniam S, Scott HL. Combined monte carlo and molecular dynamics simulation of fully hydrated dioleyl and palmitoyl-oleyl phosphatidylcholine lipid bilayers. Biophys J 1999; 77: 2462–2469
   PubMedGoogle Scholar
• Coutinho A, Prieto M. Ribonuclease T1 and alcohol dehydrogenase fluorescence quenching by acrylamide. J Chem Educ 1993; 70: 425–428
   Web of Science ®Google Scholar
• Santos NC, Castanho MA. Fluorescence spectroscopy methodologies on the study of proteins and peptides. Trends Appl Spectrosc 2002; 4: 113–125
   Google Scholar
• Caputo GA, London E. Cumulative effects of amino acid substitutions and hydrophobic mismatch upon the transmembrane stability and conformation of hydrophobic alpha-helices. Biochemistry 2003; 42: 3275–3285
   PubMed Web of Science ®Google Scholar
• Fernandes MX, Garcia de la Torre J, Castanho MA. Joint determination by Brownian dynamics and fluorescence quenching of the in-depth location profile of biomolecules in membranes. Anal Biochem 2002; 307: 1–12
   PubMedGoogle Scholar
• Santos NC, Prieto M, Castanho MA. Interaction of the major epitope region of HIV protein gp41 with membrane model systems. A fluorescence spectroscopy study. Biochemistry 1998; 37: 8674–8682
   PubMedGoogle Scholar
• Wardlaw JR, Sawyer WH, Ghiggino KP. Vertical fluctuations of phospholipid acyl chains in bilayers. FEBS Lett 1987; 223: 20–24
   PubMedGoogle Scholar
• Maier O, Oberle V, Hoekstra D. Fluorescent lipid probes: some properties and applications (a review). Chem Phys Lipids 2002; 116: 3–18
   PubMed Web of Science ®Google Scholar
• Haugland RP, 2002. Handbook of fluorescent probes and research products. 9th ed. New York: Molecular Probes.
   Google Scholar
• Pecheur EI, Martin I, Ruysschaert JM, Bienvenue A, Hoekstra D. Membrane fusion induced by 11-mer anionic and cationic peptides: a structure-function study. Biochemistry 1998; 37: 2361–2371
   PubMedGoogle Scholar
• Allison SL., Schalich J., Stiasny K., Mandl CW., Heinz FX. Mutational evidence for an internal fusion peptide in flavivirus envelope protein. E. J. Virol 2001; 75: 4268–4275
   PubMed Web of Science ®Google Scholar
• Chattopadhyay A, London E. Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 1987; 26: 39–45
   PubMed Web of Science ®Google Scholar
• Basanez G. Membrane fusion: the process and its energy suppliers. Cell Mol Life Sci 2002; 59: 1478–1490
   PubMedGoogle Scholar
• Murray D, Arbuzova A, Honig B, McLaughlin S. The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes. Curr Topics Membr 2002; 52: 271–302
   Google Scholar
• Feldman SA, Audet S, Beeler JA. The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulfate. J Virol 2000; 74: 6442–6447
   PubMed Web of Science ®Google Scholar
• Fry EE, Lea SM, Jackson T, Newman JW, Ellard FM, Blakemore WE, Abu-Ghazaleh R, Samuel A, King AM, Stuart DI. The structure and function of a foot-and-mouth disease virus-oligosaccharide receptor complex. Embo J 1999; 18: 543–554
   PubMed Web of Science ®Google Scholar
• Shukla D, Liu J, Blaiklock P, Shworak NW, Bai X, Esko JD, Cohen GH, Eisenberg RJ, Rosenberg RD, Spear PG. A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 1999; 99: 13–22
   PubMed Web of Science ®Google Scholar
• Chen Y, Maguire T, Hileman RE, Fromm JR, Esko JD, Linhardt RJ, Marks RM. Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat Med 1997; 3: 866–871
   PubMed Web of Science ®Google Scholar
• Ludtke S, He K, Huang H. Membrane thinning caused by magainin 2. Biochemistry 1995; 34: 16764–16769
   PubMed Web of Science ®Google Scholar
• Magzoub M, Graslund A. Cell-penetrating peptides: small from inception to application. Q Rev Biophys 2004; 37: 147–195
   PubMed Web of Science ®Google Scholar
• Gibbons DL, Vaney MC, Roussel A, Vigouroux A, Reilly B, Lepault J, Kielian M, Rey FA. Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature 2004; 427: 320–325
   PubMedGoogle Scholar
• Cheng SF, Wu CW, Kantchev EA, Chang DK. Structure and membrane interaction of the internal fusion peptide of avian sarcoma leukosis virus. Eur J Biochem 2004; 271: 4725–4736
   PubMedGoogle Scholar
• Chang DK, Cheng SF, Deo Trivedi V, Yang SH. The amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16–18 at the aqueous boundary at acidic pH. Oligomerization and the conformational flexibility. J Biol Chem 2000; 275: 19150–19158
   PubMed Web of Science ®Google Scholar
• Pecheur EI, Sainte-Marie J, Bienven e A, Hoekstra D. Peptides and membrane fusion: towards an understanding of the molecular mechanism of protein-induced fusion. J Membr Biol 1999; 167: 1–17
   PubMedGoogle Scholar