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Monocyte Chemotactic Protein-2 Activates Ccr5 and Blocks Cd4/Ccr5-Mediated Hiv-1 Entry/Replication

  1. Author:
    Gong, W. H.
    Howard, O. M. Z.
    Turpin, J. A.
    Grimm, M. C.
    Ueda, H.
    Gray, P. W.
    Raport, C. J.
    Oppenheim, J. J.
    Wang, J. M.
    1. Year: 1998
  2. Journal: Journal of Biological Chemistry
    1. 273
    2. 8
    3. Pages: 4289-4292
  4. Type of Article: Article
  1. Abstract:

    Human immunodeficiency virus, type I (HIV-1) cell-type tropism is dictated by chemokine receptor usage: T-cell line tropic viruses use CXCR4, whereas monocyte tropic viruses primarily use CCR5 as fusion coreceptors. CC chemokines macrophage inflammatory protein (MIP)-1 alpha, MIP-1 beta, and RANTES (regulated on activation normal T cell expressed and secreted) inhibit CD4/CCR5-mediated HIV-1 cell fusion, MCP-2 is also a member of the CC chemokine subfamily and has the capacity to interact with at least two receptors including CCR-1 and CCR2B. In an effort to further characterize the binding properties of MCP-2 on leukocytes, we observed that MCP-2, but not MCP-1, effectively competed with MIP-1 beta for binding to monocytes, suggesting that MCP-2 may interact with CCR5, As predicted, MCP-2 competitively inhibited MIP-1 beta binding to HEK293 cells stably transfected with CCR5 (CCR5/293 cells). MCP-2 also bound to and induced chemotaxis of CCR5/293 cells with a potency comparable with that of MIP-1 beta. Confocal microscopy indicates that MCP-2 caused remarkable and dose-dependent internalization of CCR5 in CCR5/ 293 cells. Furthermore, MCP-2 inhibited the entry/replication of HIV-1ADA in CCR5/293 cells coexpressing CD4. These results indicated that MCP-2 uses CCR5 as one of its functional receptors and is an additional potent natural inhibitor of HIV-1. [References: 31]

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