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N-linked glycosylation of CXCR4 masks coreceptor function for CCR5-dependent human immunodeficiency virus type 1 isolates

  1. Author:
    Chabot, D. J.
    Chen, H.
    Dimitrov, D. S.
    Broder, C. C.

  2. Author Address

    Broder CC Uniformed Serv Univ Hlth Sci, F Edward Hebert Sch Med, Dept Microbiol & Immunol 4301 Jones Bridge Rd Bethesda, MD 20814 USA Uniformed Serv Univ Hlth Sci, F Edward Hebert Sch Med, Dept Microbiol & Immunol Bethesda, MD 20814 USA NCI, Frederick Canc Res & Dev Ctr, Lab Expt & Computat Biol, NIH Frederick, MD 21702 USA
    1. Year: 2000
  2. Journal: Journal of Virology
    1. 74
    2. 9
    3. Pages: 4404-4413
  4. Type of Article: Article
  1. Abstract:

    chemokine receptors CXCR4 and CCR5 are the principal coreceptors for infection of X4 and R5 human immunodeficiency virus type 1 (HIV-1) isolates, respectively. Here we report on the unexpected observation that the removal of the N-linked glycosylation sites in CXCR4 potentially allows the protein to serve as a universal coreceptor for both X4 and R5 laboratory-adapted and primary HIV-1 strains. We hypothesize that this alteration unmasks existing common extracellular structures reflecting a conserved three-dimensional similarity of important elements of CXCR4 and CCR5 that are involved in HIV envelope glycoprotein (Env) interaction. These results may have far-reaching implications for the differential recognition of cell type-dependent glycosylated CXCR4 by HIV-1 isolates and their evolution in vivo. They also suggest a possible explanation for the various observations of restricted virus entry in some cell types and further our understanding of the framework of elements that represent the Env-coreceptor contact sites. [References: 90]

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