Skip NavigationSkip to Content
Return Return to Search Results

Structural definition of a conserved neutralization epitope on HIV-1 gp120

  1. Author:
    Zhou, T. Q.
    Xu, L.
    Dey, B.
    Hessell, A. J.
    Van Ryk, D.
    Xiang, S. H.
    Yang, X. Z.
    Zhang, M. Y.
    Zwick, M. B.
    Arthos, J.
    Burton, D. R.
    Dimitrov, D. S.
    Sodroski, J.
    Wyatt, R.
    Nabel, G. J.
    Kwong, P. D.

  2. Author Address

    NIAID, Vaccine Res Ctr, NIH, Bethesda, MD 20892 USA. NIAID, Immunoregulat Lab, NIH, Bethesda, MD 20892 USA. Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA. Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA. Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA. Harvard Univ, Sch Med, Dept Canc Immunol & AIDS, Dana Farber Canc Inst, Boston, MA 02115 USA. NCI, Ctr Canc Res, Frederick, MD 21702 USA.;Kwong, PD, NIAID, Vaccine Res Ctr, NIH, 9000 Rockville Pike, Bethesda, MD 20892 USA.;pdkwong@nih.gov
    1. Year: 2007
    2. Date: Feb
  2. Journal: Nature
    1. 445
    2. 7129
    3. Pages: 732-737
  4. Type of Article: Article
  5. ISSN: 0028-0836
  1. Abstract:

    The remarkable diversity, glycosylation and conformational flexibility of the human immunodeficiency virus type 1 (HIV-1) envelope (Env), including substantial rearrangement of the gp120 glycoprotein upon binding the CD4 receptor, allow it to evade antibody-mediated neutralization. Despite this complexity, the HIV-1 Env must retain conserved determinants that mediate CD4 binding. To evaluate how these determinants might provide opportunities for antibody recognition, we created variants of gp120 stabilized in the CD4-bound state, assessed binding of CD4 and of receptor-binding-site antibodies, and determined the structure at 2.3 angstrom resolution of the broadly neutralizing antibody b12 in complex with gp120. b12 binds to a conformationally invariant surface that overlaps a distinct subset of the CD4-binding site. This surface is involved in the metastable attachment of CD4, before the gp120 rearrangement required for stable engagement. A site of vulnerability, related to a functional requirement for efficient association with CD4, can therefore be targeted by antibody to neutralize HIV-1.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1038/nature05580
  3. View record in Web of Science®
  4. WOS: 000244205200037

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel