Inhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: Role of a conserved hydrophobic cavity in membrane fusion

Journal of Virology

Volumn 73, Issue 10, 1999, Pages 8578-8586

  Ji, Hong ^a   Shu, Wei ^a   Burling, F Temple ^a   Jiang, Shibo ^b   Lu, Min ^a  

^a WEILL CORNELL MEDICAL COLLEGE   (United States)

^b NEW YORK BLOOD CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; GLYCOPROTEIN GP 41;

ALPHA HELIX; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GENE SEQUENCE; HUMAN IMMUNODEFICIENCY VIRUS 1; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; VIRUS INFECTIVITY; VIRUS MORPHOLOGY; VIRUS MUTANT;

EID: 0032850583     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.10.8578-8586.1999     Document Type: Article

References (63)

1. Brünger, A. T. 1992. XPLOR version 3.1: a system for X-ray crystallography and NMR. Yale University Press, New Harven, Conn.
2. Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature 371:37-43.
3. Caffrey, M., M. Cai, J. Kaufman, S. J. Stahl, P. T. Wingfield, D. G. Covell, A. M. Gronenborn, and G. M. Clore. 1988. Three-dimensional solution of the 44 kDa ectodomain of SIV gp41. EMBO J. 17:4572-4584.
4. Cantor, C., and P. Schimmel. 1980. Biophysical chemistry, part III, p. 1131-1132. W. H. Freeman and Company, New York, N.Y.
5. Cao, J., L. Bergeron, E. Helseth, M. Thali, H. Repke, and J. Sodroski. 1993. Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoprotein. J. Virol. 67:2747-2755.
6. Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832.
7. Chambers, P., C. R. Pringle, and A. J. Easton. 1990. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71:3075-3080.
8. Chan, D. C., and P. S. Kim. 1998. HIV entry and its inhibition. Cell 93:681-684.
9. Chan, D. C., C. T. Chutkowski, and P. S. Kim. 1998. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. USA 95:15613-15617.
10. Chan, D. C., D. Fass, J. M. Berger, and P. S. Kim. 1997. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89:263-273.
11. Chen, C. H., T. J. Matthews, C. B. McDanal, D. P. Bolognesi, and M. L. Greenberg. 1995. A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. J. Virol. 69:3771-3777.
12. Chen, S. S., C. N. Lee, W. R. Lee, K. McIntosh, and T. H. Lee. 1993. Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein. J. Virol. 67: 3615-3619.
13. Chen, Y.-H., J. T. Yang, and K. H. Chau. 1974. Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13:3350-3359.
14. Cowtan, K. D. 1994. Joint CCP 4 and ESF-EACBM. Newsl. Protein Crystallogr. 31:34-38.
15. Crick, F. H. C. 1953. The packing of α-helices: simple coiled coils. Acta Crystallogr. 6:689-697.
16. Delwart, E. J., G. Mosialos, and T. Gilmore. 1990. Retroviral envelope glycoproteins contain a leucine zipper like repeat. AIDS Res. Hum. Retroviruses 6:703-706.
17. Dimitrov, D. S. 1997. How do viruses enter cells? The HIV coreceptors teach us a lesson of complexity. Cell 91:721-730.
18. Dubay, J. W., S. J. Roberts, B. Brody, and E. Hunter. 1992. Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. J. Virol. 66:4748-4756.
19. Edelhoch, H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
20. Ellens, H., J. Bentz, D. Mason, F. Zhang, and J. M. White. 1990. Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density. Biochemistry 29:9697-9707.
21. Evans, S. V. 1993. SETOR: hardware lighted three-dimensional solid model representation of macromolecules. J. Mol. Graphics 11:134-138.
22. Fass, D., S. C. Harrison, and P. S. Kim. 1997. Structure of Moloney murine virus envelope domain at 1.7Å resolution. Nat. Struct. Biol. 3:465-469.
23. Furuta, R. A., C. T. Wild, Y. Weng, and C. D. Weiss. 1998. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5:276-279.
24. Gallaher, W. R., J. M. Ball, R. F. Garry, M. C. Griffin, and R. C. Montelaro. 1989. A general model for the transmembrane proteins of HIV and other retroviruses. AIDS Res. Hum. Retroviruses 5:431-440.
25. Harbury, P. B., P. S. Kim, and T. Alber. 1994. Crystal structure of an isoleucine-zipper trimer. Nature 371:80-83.
26. Hernandez, L. D., L. R. Hoffman, T. G. Wolfsberg, and J. M. White. 1996. Virus-cell and cell-cell fusion. Annu. Rev. Cell Dev. Biol. 12:627-661.
27. Hughson, F. M. 1997. Enveloped viruses: a common mode of membrane fusion? Curr. Biol. 7:R565-R569.
28. Jiang, S., K. Lin, and A. R. Neurath. 1991. Enhancement of human immunodeficiency virus type 1 (HIV-1) infection by antisera to peptides from the envelope glycoprotein gp120/gp41. J. Exp. Med. 174:1557-1563.
29. Jiang, S., K. Lin, and M. Lu. 1998. A conformation-specific monoclonal antibody reacting with fusion-active gp41 from the HIV-1 envelope glycoprotein. J. Virol. 72:10213-10217.
30. Jiang, S., K. Lin, N. Strick, and A. R. Neurath. 1993. HIV-1 inhibition by a peptide. Nature 35:113.
31. Johnson, M. L., J. J. Correia, D. A. Yphantis, and H. R. Halvorson. 1981. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:575-588.
32. Jones, P. L., T. Korte, and R. Blumenthal. 1998. Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors. J. Biol. Chem. 273:404-409.
33. Jones, T. A., J. W. Zou, S. W. Cowan, and M. Kjelgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. D47:110-119.
34. Judice, J. K., J. Y. K. Tom, W. Huang, T. Wrin, J. Vennari, C. J. Petropoulos, and R. S. McDowell. 1997. Inhibition of HIV type 1 infectivity by constrained α-helical peptides: implications for the viral fusion mechanism. Proc. Natl. Acad. Sci. USA 94:13426-13430.
35. Kilby, J. M., S. Hopkins, T. M. Venetta, B. DiMassimo, G. A. Cloud, J. Y. Lee, Y. Alldredge, E. Hunter, D. Lambert, D. Bolognesi, T. Matthews, M. R. Johnson, M. A. Nowak, G. M. Shaw, and M. S. Saag. 1998. Potent suppression of HIV-1 replication in human by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat. Med. 4:1302-1307.
36. Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
37. Kwong, P. D., R. Wyatt, J. Robinson, R. W. Sweet, J. Sodroski, and W. A. Hendrickson. 1998. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648-659.
38. Laue, T. M., B. D. Shah, T. M. Ridgeway, and S. L. Pelletier. 1992. Computer-aided interpretation of analytical sedimentation data for proteins, p. 90-125. In S. E. Harding, A. J. Rowe, and J. C. Horton (ed.), Analytical ultracentrifugation in biochemistry and polymer science. Royal Society of Chemistry, Cambridge, United Kingdom.
39. Lu, M., and P. S. Kim. 1997. A trimeric structural subdomain of the HIV-1 transmembrane glycoprotein. J. Biomol. Struct. Dyn. 15:465-471.
40. Lu, M., H. Ji, and S. Shen. 1999. Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: implications for viral membrane fusion. J. Virol. 73:4433-4438.
41. Lu, M., S. C. Blacklow, and P. S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
42. Luciw, P. A. 1996. Human immunodeficiency viruses and their replication, p. 1881-1952. In B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melinick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Fields virology. Lippincott-Raven Publishers, Philadelphia, Pa.
43. Moore, J. P., B. A. Jameson, and T. Dragic. 1997. Co-receptor for HIV-1 entry. Curr. Opin. Immunol. 9:551-562.
44. Moore, J. P., B. A. Jameson, R. A. Weiss, and Q. J. Sattentau. 1993. The HIV-cell fusion reaction, p. 233-289. In J. Bentz (ed.), Viral fusion mechanisms. CRC Press, Boca Raton, Fla.
45. Munoz-Barroso, I., S. Durell, K. Sakaguchi, E. Appella, and R. Blumenthal. 1988. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J. Cell. Biol. 140:315-323.
46. Navaza, J. 1994. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50:157-163.
47. Nichols, A., K. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11:281-296.
48. Otwinowski, Z., and W. Minor. 1996. Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
49. Rimsky, L. T., D. C. Shugars, and T. J. Matthews. 1998. Determinants of human immunodeficiency virus type 1 resistance to gp41-derived inhibitory peptides. J. Virol. 72:986-993.
50. Rizzuto, C. D., R. Wyatt, N. Hernandez-Ramos, Y. Sun, P. D. Kwong, W. A. Hendrickson, and J. A. Sodroski. 1998. Conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. Science 280:1949-1953.
51. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
52. Skehel, J. J., and D. C. Wiley. 1998. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95:871-874.
53. Spruce, A. E., A. Iwata, J. M. White, and W. Almers. 1989. Patch clamp studies of single cell-fusion events mediated by a viral fusion protein. Nature 342:555-558.
54. Studier, F. W., A. H. Rosenberg, J. J. Dunn, and J. W. Dubendorff. 1990. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:60-89.
55. Sutton, R. B., D. Fasshauer, and T. A. Brunger. 1988. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395:347-353.
56. Tan, K., J. Liu, J. Wang, S. Shen, and M. Lu. 1997. Atomic structure of a thermostable subdomain of HIV-1 gp41. Proc. Natl. Acad. Sci. USA 94: 12303-12308.
57. Weissenhorn, W., A. Dessen, S. C. Harrison, J. J. Skehel, and D. C. Wiley. 1997. Atomic structure of the ectodomain from HIV-1 gp41. Nature 387: 426-430.
58. Weng, Y., and D. C. Weiss. 1998. Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 72:9676-9682.
59. White, J. M. 1992. Membrane fusion. Science 258:917-924.
60. Wild, C. T., D. C. Shugars, T. K. Greenwell, C. B. McDanal, and T. J. Matthews. 1994. Peptides corresponding to a predictive α-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proc. Natl. Acad. Sci. USA 91:9770-9774.
61. Wild, C. T., T. Greenwell, D. Shugars, L. Rimsky-Clarke, and T. J. Matthews. 1995. The inhibitory activity of an HIV-1 type peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res. Hum. Retroviruses 11:323-325.
62. Wild, C. T., T. Oas, C. B. McDanal, D. Bolognesi, and T. J. Matthews. 1992. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. USA 89:10537-10541.
63. Wiley, D. C., and J. J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-394.