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Constitutive cell surface association between CD4 and CCR5

  1. Author:
    Xiao, X. D.
    Wu, L. J.
    Stantchev, T. S.
    Feng, Y. R.
    Ugolini, S.
    Chen, H.
    Shen, Z. M.
    Riley, J. L.
    Broder, C. C.
    Sattentau, Q. J.
    Dimitrov, D. S.

  2. Author Address

    Dimitrov DS NCI, Frederick Canc Res & Dev Ctr, Lab Expt & Computat Biol, NIH Bldg 469,Room 216,POB B,Miller Dr Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, Lab Expt & Computat Biol, NIH Frederick, MD 21702 USA LeukoSite Inc Cambridge, MA 02142 USA Uniformed Serv Univ Hlth Sci, Dept Microbiol & Immunol Bethesda, MD 20814 USA Ctr Immunol Marseille Luminy F-13288 Marseille 9 France Walter Reed Army Inst Res, Dept Retroviral Rockville, MD 20850 USA
    1. Year: 1999
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 96
    2. 13
    3. Pages: 7496-7501
  4. Type of Article: Article
  1. Abstract:

    HIV-1 entry into cells involves formation of a complex between gp120 of the viral envelope glycoprotein (Env), a receptor (CD4), and a coreceptor. For most strains of HIV, this coreceptor is CCR5. Here, we provide evidence that CD4 is specifically associated with CCR5 in the absence of gp120 or any other receptor-specific ligand. The amount of CD4 coimmunoprecipitated with CCR5 was significantly higher than that with the other major HIV coreceptor, CXCR4, and in contrast to CXCR4 the CD4-CCR5 coimmunoprecipitation Was not significantly increased by gp120. The CD4-CCR5 interaction probably takes place via the second extracellular loop of CCR5 and the first two domains of CD4 It can be inhibited by CCR5- and CD4-specific antibodies that interfere with HIV-1 infection, indicating a possible role in virus entry, These findings suggest a possible pathway of HIV-1 evolution and development of immunopathogenicity, a potential new target for antiretroviral drugs and a tool for development of vaccines based on EnvCD4-CCR5 complexes. The constitutive association of a seven-transmembrane-domain G protein-coupled receptor with another receptor also indicates new possibilities for cross talk between cell surface receptors. [References: 42]

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