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HIV-1 entry and macrophage inflammatory protein-1 beta-mediated signaling are independent functions of the chemokine receptor CCR5

Academic Article
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Overview

authors

  • Farzan, Michael
  • Choe, Hyeryun
  • Martin, K. A.
  • Sun, Y.
  • Sidelko, M.
  • Mackay, C. R.
  • Gerard, N. P.
  • Sodroski, J.
  • Gerard, C.

publication date

  • March 1997

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The human immunodeficiency virus type 1 (HIV-1) requires the presence of specific chemokine receptors in addition to CD4 to enter its target cell. The chemokine receptor CCR5 is used by macrophage-tropic strains of HIV-1, which predominate during the asymptomatic stages of infection. Here we investigate whether the ability of CCR5 to signal in response to its beta-chemokine ligands is necessary or sufficient for viral entry. Three CCR5 mutants with little or no ability to mobilize calcium in response to macrophage inflammatory protein-1beta could nonetheless support HIV-1 entry and the early steps in the virus life cycle with efficiencies comparable with those of wild-type CCR5. Conversely, a chimeric receptor with the N terminus of CCR2 replacing that of CCR5 responded to macrophage inflammatory protein-1beta and MCP-1 but did not efficiently support viral entry. These results demonstrate that chemokine signaling and HIV-1 entry are separable functions of CCR5 and that only viral entry requires the N-terminal domain of CCR5.

subject areas

  • Animals
  • Cell Line
  • Chemokine CCL4
  • Dogs
  • HIV-1
  • Humans
  • Macrophage Inflammatory Proteins
  • Macrophages
  • Mutation
  • Receptors, CCR5
  • Receptors, Cytokine
  • Receptors, HIV
  • Signal Transduction
  • Virus Replication
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 9054370
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Additional Document Info

start page

  • 6854

end page

  • 6857

volume

  • 272

issue

  • 11

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