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Viral macrophage inflammatory protein-II (vMIP) is a highly basic protein and human chemokine analog encoded by human herpesvirus-8. The structure of vMIP consists of 71 residues and is a monomer under most conditions. It helps its virus evade the host immune system through selectively blocking and activating different receptors, preferentially inhibiting acute Th1-associated inflammation while also upregulating Th2 associated immune response.
Viral macrophage inflammatory protein-II (vMIP) is a highly basic protein and human chemokine analog encoded by human herpesvirus-8. The structure of vMIP consists of 71 residues and is a monomer under most conditions. It helps its virus evade the host immune system through selectively blocking and activating different receptors, preferentially inhibiting acute Th1-associated inflammation while also upregulating Th2 associated immune response.
This protein has the ability to bind to chemokine receptors (including both HIV coreceptors) and cell surface glycosaminoglycans. At the chemokine receptors, vMIP acts as an antagonist at CCR1, CCR2, CCR5, and CXCR4 while it is an agonist at CCR3 and CCR8. Due to its antagonistic action at CCR5 and CXCR4, vMIP is able to block HIV cell entry through these coreceptors while also inhibiting inflammation of monocytes and Th1 type T cells -- both major targets for HIV-1 and thus vMIP has potential to act as an HIV inhibitor. Glycosaminoglycans, on the other hand, are important as the binding to glycosaminoglycans may be essential for the protein to carry out its natural function in vivo. vMIP is angiogenic -- its pro-angiogenic capabilities in mature and progenitor endothelial cells gives it potential for use in organ transplantations. It is also selectively chemotactic for Th2 lymphocytes. Overall, the major role of vMIP-II is regulation of immune responses.
