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