Characterization of the interactions of vMIP-II, and a dimeric variant of vMIP-II, with glycosaminoglycans.

ABSTRACT: Chemokines are important immune proteins, carrying out their function by binding to glycosaminoglycans (GAGs) on the endothelial surface and to cell surface chemokine receptors. A unique viral chemokine analogue, viral macrophage inflammatory protein-II (vMIP-II), encoded by human herpesvirus-8, has garnered interest because of its ability to bind to multiple chemokine receptors, including both HIV coreceptors. In addition, vMIP-II binds to cell surface GAGs much more tightly than most human chemokines, which may be the key to its anti-inflammatory function in vivo. The goal of this work was to determine the mechanism of binding of GAG by vMIP-II. The interaction of vMIP-II with a heparin-derived disaccharide was characterized using NMR. Important binding sites were further analyzed by mut

SUBMITTER: Zhao B 

PROVIDER: S-EPMC2924879 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature