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A tyrosine-rich region in the N terminus of CCR5 is important for human immunodeficiency virus type 1 entry and mediates an association between gp120 and CCR5

Academic Article
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Overview

authors

  • Farzan, Michael
  • Choe, Hyeryun
  • Vaca, L.
  • Martin, K.
  • Sun, Y.
  • Desjardins, E.
  • Ruffing, N.
  • Wu, L. J.
  • Wyatt, Richard
  • Gerard, N.
  • Gerard, C.
  • Sodroski, J.

publication date

  • February 1998

journal

  • Journal of Virology  Journal

abstract

  • Human immunodeficiency virus type 1 (HIV-1) requires the presence of specific chemokine receptors in addition to CD4 to enter target cells. The chemokine receptor CCR5 is used by the macrophage-tropic strains of HIV-1 that predominate during the asymptomatic stages of infection. Here we identify a small tyrosine-rich region of CCR5 proximal to the N-terminal cysteine that is critical for entry of macrophage-tropic and dual-tropic variants of HIV-1. HIV-1 infection of cells expressing CCR5 mutants with changes in this region was substantially reduced compared with the infection of cells bearing wild-type CCR5. Simian immunodeficiency virus (SIVmac239) entry was also ablated on a subset of these mutants but enhanced on others. These differences in virus entry were correlated with the relative ability of soluble, monomeric HIV-1 and SIVmac239 gp120 glycoproteins to bind the CCR5 mutants. These results identify a region of CCR5 that is necessary for the physical association of the gp120 envelope glycoprotein with CCR5 and for HIV-1 infection.

subject areas

  • Animals
  • Binding Sites
  • Cell Line
  • Dogs
  • HIV Envelope Protein gp120
  • HIV Infections
  • HIV-1
  • Humans
  • Mutation
  • Receptors, CCR5
  • Tyrosine
  • Virus Replication
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Identity

PubMed Central ID

  • PMC124591

International Standard Serial Number (ISSN)

  • 0022-538X

PubMed ID

  • 9445013
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Additional Document Info

start page

  • 1160

end page

  • 1164

volume

  • 72

issue

  • 2

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