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Increased association of glycoprotein 120-CD4 with HIV type 1 coreceptors in the presence of complex-enhanced anti-CD4 monoclonal antibodies

  1. Author:
    Golding, H.
    Ouyang, J.
    Zaitseva, M.
    Broder, C. C.
    Dimitrov, D. S.
    Lapham, C.

  2. Author Address

    Golding H US FDA, Div Viral Prod, CBER Bldg 29B,Room 4NN04,8800 Rockville Pike Bethesda, MD 20892 USA US FDA, Div Viral Prod, CBER Bethesda, MD 20892 USA NCI, Sect Membrane Struct & Funct, FCRDC, NIH Frederick, MD 21702 USA Uniformed Serv Univ Hlth Sci, Dept Microbiol & Immunol Bethesda, MD 20814 USA
    1. Year: 1999
  2. Journal: Aids Research and Human Retroviruses
    1. 15
    2. 2
    3. Pages: 149-159
  4. Type of Article: Article
  1. Abstract:

    CD4-specific monoclonal antibodies (CG1, CG7, and CG8), which bind,vith a 5- to 10-fold higher avidity to preformed CD4-gp120 complexes than to CD4, were previously shown to recognize newly identified conformational epitopes in the D1-CDR3 region of CD4, In the current study, these and other complex-enhanced MAbs were tested in three separate assays of HIV-1 coreceptor (CXCR4/CCR5) recruitment. In these assays, the CD4-specific MAbs CG1, -7, and -8 stabilized the association of coreceptor, gp120, and CD4 in trimolecular complexes. In contrast, the gp120-specific, complex-enhanced MAbs 48d and 17b were inhibitory. These data suggest that conformational changes in the CDR3 region of CD4-D1, induced by gp120 binding, may be involved in coreceptor association and thus play a positive role in the HIV-1 cell fusion process. [References: 30]

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