A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 36, 2009, Pages 15314-15319

  Qiang, Wei ^a   Sun, Yan ^a   Weliky, David P ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

AIDS; Enveloped virus; Location; NMR; Trimer

Indexed keywords

CARBONYL DERIVATIVE; CHOLESTEROL; GLYCOPROTEIN GP 41; LIPID; MONOMER; VIRUS FUSION PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; BILAYER MEMBRANE; CELL NUCLEUS; GENE CONSTRUCT; GENE FUSION; GENE INSERTION; GENE MUTATION; GENE SEQUENCE; HUMAN IMMUNODEFICIENCY VIRUS; MEMBRANE FUSION; MEMBRANE VESICLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OLIGOMERIZATION; PRIORITY JOURNAL;

CELL MEMBRANE; HIV ENVELOPE PROTEIN GP41; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; VIRUS ATTACHMENT;

EID: 70349304444     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0907360106     Document Type: Article

References (22)

1. White JM, Delos SE, Brecher M, Schornberg K (2008) Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme. Crit Rev Biochem Mol Biol 43:189-219. (Pubitemid 351883153)
2. Freed EO, Delwart EL, Buchschacher GL, Jr., Panganiban AT (1992) A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proc Natl Acad Sci USA 89:70-74.
3. Durell SR, Martin I, Ruysschaert JM, Shai Y, Blumenthal R (1997) What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion. Mol Membr Biol 14:97-112. (Pubitemid 27478674)
4. Li YL, Tamm LK (2007) Structure and plasticity of the human immunodeficiency virus gp41 fusion domain in lipid micelles and bilayers. Biophys J 93:876-885.
5. Nieva JL, Nir S, Muga A, Goni FM, Wilschut J (1994) Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage. Biochemistry 33:3201-3209. (Pubitemid 24112630)
6. Reichert J, et al. (2007) A critical evaluation of the conformational requirements of fusogenic peptides in membranes. Eur Biophys J 36:405-413. (Pubitemid 46626198)
7. Yang R, Prorok M, Castellino FJ, Weliky DP (2004) A trimeric HIV-1 fusion peptide construct which does not self-associate in aqueous solution and which has 15-fold higher membrane fusion rate. J Am Chem Soc 126:14722-14723. (Pubitemid 39532144)
8. Gordon LM, et al. (1992) The amino-terminal peptide of HIV-1 glycoprotein 41 interacts with human erythrocyte membranes: Peptide conformation, orientation and aggregation. Biochim Biophys Acta 1139:257-274.
9. Agirre A, et al. (2000) Interactions of the HIV-1 fusion peptide with large unilamellar vesicles and monolayers. A cryo-TEM and spectroscopic study. Biochim Biophys Acta 1467:153-164.
10. Haque ME, Koppaka V, Axelsen PH, Lentz BR (2005) Properties and structures of the influenza and HIV fusion peptides on lipid membranes: Implications for a role in fusion. Biophys J 89:3183-3194. (Pubitemid 41636073)
11. Pereira FB, Goni FM, Muga A, Nieva JL (1997) Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: Dose and sequence effects. Biophys J 73:1977-1986. (Pubitemid 27425728)
12. Jaroniec CP, et al. (2005) Structure and dynamics of micelle-associated human immunodeficiency virus gp41 fusion domain. Biochemistry 44:16167-16180.
13. Brugger B, et al. (2006) The HIV lipidome: A raft with an unusual composition. Proc Natl Acad Sci USA 103:2641-2646. (Pubitemid 43306602)
14. Qiang W, Bodner ML, Weliky DP (2008) Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries. J Am Chem Soc 130:5459-5471. (Pubitemid 351612954)
15. Qiang W, Weliky DP (2009) HIV fusion peptide and its cross-linked oligomers: Efficient syntheses, significance of the trimer in fusion activity, correlation of β strand conformation with membrane cholesterol, and proximity to lipid headgroups. Biochemistry 48:289-301.
16. Kamath S, Wong TC (2002) Membrane structure of the human immunodeficiency virus gp41 fusion domain by molecular dynamics simulation. Biophys J 83:135-143. (Pubitemid 34694726)
17. Maddox MW, Longo ML (2002) Conformational partitioning of the fusion peptide of HIV-1 gp41 and its structural analogs in bilayer membranes. Biophys J 83:3088-3096.
18. Toke O, Maloy WL, Kim SJ, Blazyk J, Schaefer J (2004) Secondary structure and lipid contact of a peptide antibiotic in phospholipid bilayers by REDOR. Biophys J 87:662-674. (Pubitemid 38880119)
19. Qiang W, Yang J, Weliky DP (2007) Solid-state nuclear magnetic resonance measurements of HIV fusion peptide to lipid distances reveal the intimate contact of beta strand peptide with membranes and the proximity of the Ala-14-Gly-16 region with lipid headgroups. Biochemistry 46:4997-5008. (Pubitemid 46682998)
20. Zheng Z, Yang R, Bodner ML, Weliky DP (2006) Conformational flexibility and strand arrangements of the membrane-associated HIV fusion peptide trimer probed by solid-state NMR spectroscopy. Biochemistry 45:12960-12975. (Pubitemid 44763419)
21. βI) phase lipid bilayers in constant pressure and constant surface area ensembles. J Chem Phys 112:4822-4832.
22. Bloom M, Evans E, Mouritsen OG (1991) Physical properties of the fluid lipid-bilayer component of cell membranes: A perspective. Q Rev Biophys 24:293-397. (Pubitemid 121000390)