Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry - PubMed (original) (raw)

Comparative Study

. 1999 Mar 5;96(5):667-76.

doi: 10.1016/s0092-8674(00)80577-2.

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Comparative Study

Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry

M Farzan et al. Cell. 1999.

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Abstract

Chemokine receptors and related seven-transmembrane-segment (7TMS) receptors serve as coreceptors for entry of human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV) into target cells. Each of these otherwise diverse coreceptors contains an N-terminal region that is acidic and tyrosine rich. Here, we show that the chemokine receptor CCR5, a principal HIV-1 coreceptor, is posttranslationally modified by O-linked glycosylation and by sulfation of its N-terminal tyrosines. Sulfated tyrosines contribute to the binding of CCR5 to MIP-1 alpha, MIP-1 beta, and HIV-1 gp120/CD4 complexes and to the ability of HIV-1 to enter cells expressing CCR5 and CD4. CXCR4, another important HIV-1 coreceptor, is also sulfated. Tyrosine sulfation may contribute to the natural function of many 7TMS receptors and may be a modification common to primate immunodeficiency virus coreceptors.

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