Structure of an HIV gp 120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

Nature

Volumn 393, Issue 6686, 1998, Pages 648-659

  Kwong, Peter D ^a   Wyatt, Richard ^b,c   Robinson, James ^d   Sweet, Raymond W ^e   Sodroski, Joseph ^b,c   Hendrickson, Wayne A ^a  

^a Columbia University ^*  (United States)

^b HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

^c HARVARD MEDICAL SCHOOL   (United States)

^d TULANE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e GLAXOSMITHKLINE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; CHEMOKINE RECEPTOR; GLYCOPROTEIN GP 120; NEUTRALIZING ANTIBODY; CHEMOKINE RECEPTOR CCR5; GLYCOPROTEIN GP 41; HUMAN IMMUNODEFICIENCY VIRUS ANTIBODY; IMMUNOGLOBULIN FRAGMENT;

BINDING SITE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; HUMAN; HUMAN IMMUNODEFICIENCY VIRUS; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; REVIEW; VIRUS NEUTRALIZATION; AMINO ACID SEQUENCE; ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CHO CELL; CRICETULUS; GLYCOSYLATION; HAMSTER; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; SERODIAGNOSIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; ANTIGENS, CD4; CHO CELLS; CRICETINAE; CRICETULUS; CRYSTALLOGRAPHY, X-RAY; GLYCOSYLATION; HIV ANTIBODIES; HIV ENVELOPE PROTEIN GP120; HIV ENVELOPE PROTEIN GP41; HUMANS; IMMUNOGLOBULIN FRAGMENTS; MEMBRANE FUSION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEUTRALIZATION TESTS; PROTEIN CONFORMATION; RECEPTORS, CCR5;

EID: 0032543307     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/31405     Document Type: Review

References (50)

1. Barre-Sinoussi, F. et al. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immunodeficiency syndrome (AIDS). Science 220, 868-871 (1983).
2. Gallo, R. C. et al Frequent detection and isolation of cytopathic retroviruses (HTLV-III) from patients with AIDS and at risk for AIDS. Science 224, 500-503 (1984).
3. Kowalski, M. L. et al. Functional regions of the envelope glycoprotein of human immunodeficiency virus type 1. Science 237, 1351-1355 (1987).
4. Lu, M., Blackow, S. & Kim, P. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Struct. Biol 2, 1075-1082 (1995).
5. Starcich, B. R. et al Identification and characterization of conserved and variable regions of the envelope gene HTLV-III/LAV, the retrovirus of AIDS. Cell 45, 637-648 (1986).
6. Leonard, C. K. et al. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cell. J. Biol. Chem. 265, 10373-10382 (1990).
7. Profy, A. T. et al. Epitopes recognized by the neutralizing antibodies of an HIV-1-infected individual. J. Immunol. 144, 4641-4647 (1990).
8. Ryu, S.-E. et al Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature 348, 419-426 (1990).
9. Wang, J. H. et al. Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Nature 348, 411-418 (1990).
10. Wu, H., Kwong, P. D. & Hendrickson, W. A. Dimeric association and segmental variability in the structure of human CD4. Nature 387, 527-530 (1997).
11. Moebius, U., Clayton, L., Abraham, S., Harrison, S. & Reinhertz, E. The human immunodeficiency virus gp120 binding site of CD4: Delineation by quantitative equilibrium and kinetic binding studies of mutants in conjunction with a high-resolution CD4 atomic structure. J. Exp. Med. 176, 507-517 (1992).
12. Sweet, R. W., Truneh, A. & Hendrickson, W. A. CD4: its structure, role in immune function and AIDS pathogenesis, and potential as a pharmacologicla target. Curr. Opin. Biotech, 2, 622-633 (1991).
13. Olshevsky, U. et al. Identification of individual HIV-1 gp120 amino acids important for CD4 receptor binding. J. Virol. 64 (1990).
14. Cordonnier, A., Montagnier, L. & Emerman, M. Single amino-acid changes in HIV envelope affect viral tropism and receptor binding. Nature 340, 571-574 (1989).
15. Moore, J. P. Coreceptors: implications for HIV pathogenesis and therapy. Science 276, 51-52 (1997).
16. Feng, F., Broder, C. C, Kennedy, P. E. & Berger, E. A. HIV-1-entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science 272, 872-877 (1996).
17. Speck, R. F. et al Selective employment of chemokine receptors as human immunodeficiency virus type 1 coreceptors determined by individual amino acids in the envelope V3 loop. J. Virol. 71, 7136-7139 (1997).
18. Thali, M. et al. Characterization of conserved human immunodeficiency virus type 1 (HIV-1) gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol. 67, 3978-3988 (1993).
19. Sattentau, Q. J., Moore, J. P., Vignaux, F., Traincard, F. & Poignard, P. Conformational changes induced in the envelope glycoproteins of human and simian immunodeficiency virus by soluble receptor binding. J. Virol. 64, 7383-7383 (1993).
20. Wu, L. et al CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR5. Nature 384, 179-183 (1996).
21. Moore, J. P., McKeating, J. A., Weiss, R. A, & Sattentau, Q, J. Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science 250, 1139-1142 (1990).
22. Bullough, P A., Hughson, F. M., Skehel, J. J. & Wiley, D. C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43 (1994).
23. Fass, D. et al Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 Ångström resolution. Science 277, 1662-1666 (1997).
24. Wyatt, R. et al. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature 393, 705-711 (1998).
25. Kwong, P. D. et al. Quantitative probability analysis and variational crystallization of gp120, the exterior envelope glycoprotein of the human immunodeficiency virus type 1 (HIV-1). J. Biol. Chem. (submitted).
26. Binley, J. M. et al. Analysis of the interaction of antibodies with a conserved, enzymatically deglycosylated core of the HIV-1 gp120 envelope glycoprotein. AIDS Res. Hum. Retrovir. 14, 191-198 (1997).
27. Leesong, M., Hederson, B. S., Gillig, J. R., Schwab, J. M. & Smith, J. L. Structure of a dehydrataseisomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site. Structure 4, 253-264 (1996).
28. Cedergren-Zeppezauer, E. S., Larsson, G., Nyman, P. O., Dauter, Z. & Wilson, K. S. Crystal structure of a dUTPase. Nature 355, 740-743 (1992).
29. Ryu, S.-E., Truneh, A., Sweet, R. W. & Hendrickson, W. A. Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices. Structure 2, 59-74 (1994).
30. Rizzuto, C. et al. A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding. Science (in the press).
31. Dragic, T. et al. Amino-terminal substitutions in the CCR5 coreceptor impair gp120 binding and human immunodeficiency type 1 entry. J. Virol. 72, 279-285 (1998).
32. Farzan, M. et al. A tryosine-rich region in the N-terminus of CCR5 is important for human immunodeficiency virus type 1 entry and mediates an association between gp120 and CCR5. J. Virol. 72, 1160-1164 (1998).
33. Wyatt, R. et al. Analysis of the interaction of the human immunodeficiency virus type 1 gp120 envelope glycoprotein with the gp41 transmembrane glycoprotein. J. Virol. 71, 9722-9731 (1997).
34. Helseth, E., Olshevsky, U., Furman, C. & Sodroski, J. Human immunodeficiency virus type 1 gp120 envelope glycoprotein regions important for association with the gp41 transmembrane glycoprotein. J. Virol. 65, 2119-2123 (1991).
35. Wilson, I. A., Skehel, J. J. & Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366-373 (1981).
36. Wyatt, R. et al. Involvement of the V1/V2 variable loop structure in the exposure of human immunodeficiency virus type 1 gp120 epitopes induced by receptor binding. J. Virol. 69, 5723-5733 (1995).
37. Rost, B., Sander, C. & Schneider, R. PHD - an automated mail server for protein secondary structure prediction. Comput. Appl Biosci. 10, 53-60 (1994).
38. Wyatt, R. et al. Functional and immunologic characterization of human immunodeficiency virus type 1 envelope glycoproteins containing deletions of the major variable regions. J. Virol. 67, 4557-4565 (1993).
39. Wu, H. et al. Kinetic and structural analysis of mutant CD4 receptors that are defective in HIV gp120 binding. Proc. Natl Acad. Sci. USA 93, 15030-15035 (1996).
40. Chan, D. C., Fass, D., Berger, J. M. & Kim, P. S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273 (1997).
41. Weissenhorn, W., Dessen, A., Harrison, S. C., Skehel, J. J. & Wiley, D. C. Atomic structure of the ectodomain from HIV-1 gp41. Nature 387, 426-430 (1997).
42. Dumonceaux, J. et al. Spontaneous mutations in the env gene of the human immunodeficiency virus type 1 NDK isolate are associated with a CD4-independent entry phenotype. J. Virol. 72, 519-519 (1998).
43. Moir, S., Perreault, J. & Poulin, L. Postbinding events mediated by human immunodeficiency virus type 1 are sensitive to modifications in the D4-transmembrane linked region of CD4. J. Virol. 70, 8019-8028 (1996).
44. Kohlstaadt, L. A., Wang, J., Friedman, J. M., Rice, P. A. & Steitz, T. A. Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256, 1783-1790 (1992).
45. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Meth. Enymol. 276, 307-326 (1997).
46. Brunger, A. T. XPLOR Version 3.1 manual (Yale University, New Haven, 1993).
47. Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
48. Zhu, X. et al Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614 (1996).
49. Carson, M. Ribbons 2.0. J. Appl. Crystallogr. 24, 958-961 (1991)
50. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insight from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).