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. 1997 Sep;71(9):7136–7139. doi: 10.1128/jvi.71.9.7136-7139.1997

Selective employment of chemokine receptors as human immunodeficiency virus type 1 coreceptors determined by individual amino acids within the envelope V3 loop.

R F Speck 1, K Wehrly 1, E J Platt 1, R E Atchison 1, I F Charo 1, D Kabat 1, B Chesebro 1, M A Goldsmith 1
PMCID: PMC192016  PMID: 9261451

Abstract

The chemokine receptor CCR5 acts as an essential cofactor for cell entry by macrophage-tropic human immunodeficiency virus type 1 (HIV-1) strains, whereas CXCR4 acts as an essential cofactor for T-cell-line-adapted strains. We demonstrated that the specific amino acids in the V3 loop of the HIV-1 envelope protein that determine cellular tropism also regulate chemokine coreceptor preference for cell entry by the virus. Further, a strong correlation was found between HIV-1 strains classified as syncytium inducing in standard assays and those using CXCR4 as a coreceptor. These data support the hypothesis that progressive adaptation to additional coreceptors is a key molecular basis for HIV-1 phenotypic evolution in vivo.

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Selected References

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