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Structural Basis of Immune Evasion at the Site of CD4 Attachment on HIV-1 gp120

  1. Author:
    Chen, L.
    Kwon, Y. D.
    Zhou, T. Q.
    Wu, X. L.
    O'Dell, S.
    Cavacini, L.
    Hessell, A. J.
    Pancera, M.
    Tang, M.
    Xu, L.
    Yang, Z. Y.
    Zhang, M. Y.
    Arthos, J.
    Burton, D. R.
    Dimitrov, D. S.
    Nabel, G. J.
    Posner, M. R.
    Sodroski, J.
    Wyatt, R.

  2. Author Address

    Chen, Lei, Kwon, Young Do, Zhou, Tongqing, Wu, Xueling, O'Dell, Sijy, Pancera, Marie, Tang, Min, Xu, Ling, Yang, Zhi-Yong, Nabel, Gary J.; Wyatt, Richard, Mascola, John R.; Kwong, Peter D.] NIAID, Vaccine Res Ctr, NIH, Bethesda, MD 20892 USA. [Cavacini, Lisa, Posner, Marshall R.] Harvard Univ, Sch Med, Dana Farber Canc Inst, Head & Neck Oncol Program, Boston, MA 02115 USA. [Hessell, Ann J.; Burton, Dennis R.] Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA. [Hessell, Ann J.; Burton, Dennis R.] Scripps Res Inst, Dept Microbial Sci, La Jolla, CA 92037 USA. [Hessell, Ann J.; Burton, Dennis R.] Scripps Res Inst, Int AIDS Vaccine Initiat Neutralizing Antibody Ct, La Jolla, CA 92037 USA. [Zhang, Mei-Yun, Dimitrov, Dimiter S.] NCI, Ctr Canc Res, Frederick, MD 21702 USA. [Arthos, James] NIAID, Immunoregulat Lab, NIH, Bethesda, MD 20892 USA. [Burton, Dennis R.] Massachusetts Gen Hosp, MIT, Ragon Inst, Boston, MA 02114 USA. [Burton, Dennis R.] Harvard Univ, Boston, MA 02114 USA. [Sodroski, Joseph] Harvard Univ, Sch Med, Dana Farber Canc Inst, Dept Canc Immunol & AIDS, Boston, MA 02115 USA.
    1. Year: 2009
  2. Journal: Science
    1. 326
    2. 5956
    3. Pages: 1123-1127
  4. Type of Article: Article
  5. ISSN: 0036-8075
  1. Abstract:

    The site on HIV-1 gp120 that binds to the CD4 receptor is vulnerable to antibodies. However, most antibodies that interact with this site cannot neutralize HIV-1. To understand the basis of this resistance, we determined co-crystal structures for two poorly neutralizing, CD4-binding site (CD4BS) antibodies, F105 and b13, in complexes with gp120. Both antibodies exhibited approach angles to gp120 similar to those of CD4 and a rare, broadly neutralizing CD4BS antibody, b12. Slight differences in recognition, however, resulted in substantial differences in F105- and b13-bound conformations relative to b12-bound gp120. Modeling and binding experiments revealed these conformations to be poorly compatible with the viral spike. This incompatibility, the consequence of slight differences in CD4BS recognition, renders HIV-1 resistant to all but the most accurately targeted antibodies.

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  2. DOI: 10.1126/science.1175868
  3. PMID: 19965434

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