The antigenic structure of the HIV gp120 envelope glycoprotein View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1998-06

AUTHORS

Richard Wyatt, Peter D. Kwong, Elizabeth Desjardins, Raymond W. Sweet, James Robinson, Wayne A. Hendrickson, Joseph G. Sodroski

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. More... »

PAGES

705-711

Journal

TITLE

Nature

ISSUE

6686

VOLUME

393

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/31514

    DOI

    http://dx.doi.org/10.1038/31514

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1007469332

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/9641684


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    27 schema:description 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.
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    47 chemokine receptors
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    52 crystal structure
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    54 elicits
    55 entry
    56 envelope complex
    57 envelope glycoprotein
    58 epitope map
    59 epitopes
    60 exterior envelope glycoprotein
    61 fraction
    62 glycoprotein
    63 gp120
    64 gp120 core
    65 gp120 envelope glycoprotein
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    67 gp120 glycoprotein
    68 gp120 region
    69 gp41
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    75 infection
    76 interaction
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    78 loop structure
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    82 neutralization epitopes
    83 non-neutralizing antibodies
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    86 receptor-binding region
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    90 sequential interactions
    91 spatial organization
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