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The antigenic structure of the HIV gp120 envelope glycoprotein

Author

Listed:
  • Richard Wyatt

    (Dana-Farber Cancer Institute, Harvard Medical School)

  • Peter D. Kwong

    (Howard Hughes Medical Institute, Columbia University)

  • Elizabeth Desjardins

    (Dana-Farber Cancer Institute, Harvard Medical School)

  • Raymond W. Sweet

    (SmithKline Beecham Pharmaceuticals)

  • James Robinson

    (Tulane University Medical Center)

  • Wayne A. Hendrickson

    (Howard Hughes Medical Institute, Columbia University)

  • Joseph G. Sodroski

    (Dana-Farber Cancer Institute, Harvard Medical School
    Harvard School of Public Health)

Abstract

The human immunodeficiency virus HIV-1 establishes persistent infections in humans which lead to acquired immunodeficiency syndrome (AIDS). The HIV-1 envelope glycoproteins, gp120 and gp41, are assembled into a trimeric complex that mediates virus entry into target cells1. HIV-1 entry depends on the sequential interaction of the gp120 exterior envelope glycoprotein with the receptors on the cell, CD4 and members of the chemokine receptor family2,3,4. The gp120 glycoprotein, which can be shed from the envelope complex, elicits both virus-neutralizing and non-neutralizing antibodies during natural infection. Antibodies that lack neutralizing activity are often directed against the gp120 regions that are occluded on the assembled trimer and which are exposed only upon shedding5,6. Neutralizing antibodies, by contrast, must access the functional envelope glycoprotein complex7 and typically recognize conserved or variable epitopes near the receptor-binding regions8,9,10,11. Here we describe the spatial organization of conserved neutralization epitopes on gp120, using epitope maps in conjunction with the X-ray crystal structure of a ternary complex that includes a gp120 core, CD4 and a neutralizing antibody12. A large fraction of the predicted accessible surface of gp120 in the trimer is composed of variable, heavily glycosylated core and loop structures that surround the receptor-binding regions. Understanding the structural basis for the ability of HIV-1 to evade the humoral immune response should assist in the design of a vaccine.

Suggested Citation

  • Richard Wyatt & Peter D. Kwong & Elizabeth Desjardins & Raymond W. Sweet & James Robinson & Wayne A. Hendrickson & Joseph G. Sodroski, 1998. "The antigenic structure of the HIV gp120 envelope glycoprotein," Nature, Nature, vol. 393(6686), pages 705-711, June.
  • Handle: RePEc:nat:nature:v:393:y:1998:i:6686:d:10.1038_31514
    DOI: 10.1038/31514
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    Cited by:

    1. Durgadevi Parthasarathy & Karunakar Reddy Pothula & Sneha Ratnapriya & Héctor Cervera Benet & Ruth Parsons & Xiao Huang & Salam Sammour & Katarzyna Janowska & Miranda Harris & Joseph Sodroski & Priyam, 2024. "Conformational flexibility of HIV-1 envelope glycoproteins modulates transmitted/founder sensitivity to broadly neutralizing antibodies," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Swetha Garimalla & Thomas Kieber-Emmons & Anastas D Pashov, 2015. "The Patterns of Coevolution in Clade B HIV Envelope's N-Glycosylation Sites," PLOS ONE, Public Library of Science, vol. 10(6), pages 1-18, June.
    3. Dongxiao Han & Liuquan Sun & Yanqing Sun & Li Qi, 2017. "Mark-specific additive hazards regression with continuous marks," Lifetime Data Analysis: An International Journal Devoted to Statistical Methods and Applications for Time-to-Event Data, Springer, vol. 23(3), pages 467-494, July.
    4. Shixia Wang & Kun-Wei Chan & Danlan Wei & Xiuwen Ma & Shuying Liu & Guangnan Hu & Saeyoung Park & Ruimin Pan & Ying Gu & Alexandra F. Nazzari & Adam S. Olia & Kai Xu & Bob C. Lin & Mark K. Louder & Kr, 2024. "Human CD4-binding site antibody elicited by polyvalent DNA prime-protein boost vaccine neutralizes cross-clade tier-2-HIV strains," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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