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    Biochem Biophys Res Commun. 2000 Feb 24;268(3):938-41.

    Identification of viral macrophage inflammatory protein (vMIP)-II as a ligand for GPR5/XCR1.

    Shan L, Qiao X, Oldham E, Catron D, Kaminski H, Lundell D, Zlotnik A, Gustafson E, Hedrick JA.

    Human Genome Research, Schering-Plough Research Institute, Kenilworth, New Jersey 07033, USA.

    Lymphotactin is unique among chemokines in that it contains only two of four conserved cysteines and may possess a structure less constrained than other chemokines. The viral chemokine vMIP-II, which presumably has a structure similar to that of CC chemokines has been shown to inhibit many chemokine receptors, but its activity at GPR5/XCR1 has not been described. Interestingly, vMIP-II (but not vMIP-I) was found to be a potent antagonist of lymphotactin activity at GPR5/XCR1, extending the range of chemokine classes that this viral protein is known to inhibit to include the C class chemokine. In addition, we have extended previous analyses of GPR5/XCR1 expression and show that this receptor is expressed in leukocyte cells previously shown to be responsive to lymphotactin. Copyright 2000 Academic Press.

    PMID: 10679309 [PubMed - indexed for MEDLINE]

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