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J Biol Chem, Vol. 274, Issue 31, 21569-21574, July 30, 1999
From the Divisions of Discovery Biology and Molecular Pharmacology,
ChemoCentryx, San Carlos, California 94070
Uncertainty regarding viral chemokine function is
mirrored by an incomplete knowledge of host chemokine receptor usage by the virally encoded proteins. One such molecule is vMIP-I, a C-C type
chemokine of undefined function and binding specificity, encoded by the
Kaposi's sarcoma herpesvirus HHV-8. We report here that vMIP-I binds
to and induces cytosolic [Ca2+] signals in human T
cells selectively through CCR8, a CC chemokine receptor associated with
Th2 lymphocytes. Furthermore, using a panel of 65 different human,
viral, and rodent chemokines, we have established a comprehensive
ligand binding "fingerprint" for CCR8. The receptor exhibits marked
"high" affinity (Kd < 15 nM) only
for four chemokines, three of them of viral origin: vMIP-I, vMIP-II,
vMCC-I, and human I-309. A previously unreported second class of lower
affinity ligands includes MCP-3 and possibly two other viral
chemokines. vMIP-I and I-309 appear to act as CCR8 agonists: binding to
and inducing cytosolic [Ca2+] elevation through the
receptor. By contrast, vMIP-II and vMCC-I act as potent antagonists:
binding without inducing signaling, and blocking the effects of I-309
and vMIP-I. These results suggest a ligand hierarchy for CCR8,
identifying vMIP-I as a selective viral chemokine agonist. CCR8 may
thus engage a specific subset of chemokines with the potential to
regulate each other during viral infection and immune regulation.
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