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

Article Details

Citation

Farzan M, Mirzabekov T, Kolchinsky P, Wyatt R, Cayabyab M, Gerard NP, Gerard C, Sodroski J, Choe H

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

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

PubMed ID
10089882 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
C-C chemokine receptor type 5P51681Details
C-X-C chemokine receptor type 4P61073Details