Sequence, evolution and ligand binding properties of mammalian Duffy antigen/receptor for chemokines

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dc.contributor.authorTournamille, C.
dc.contributor.authorBlancher, A.
dc.contributor.authorLe van Kim, C.
dc.contributor.authorGane, P.
dc.contributor.authorApoil, P. A.
dc.contributor.authorNakamoto, W.
dc.contributor.authorCartron, J. P.
dc.contributor.authorColin, Y.
dc.contributor.institutionInst Natl Transfus Sanguine
dc.contributor.institutionUniv Toulouse 3
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:27:04Z
dc.date.available2014-05-20T15:27:04Z
dc.date.issued2004-01-01
dc.description.abstractThe Duffy antigen/receptor for chemokine, DARC, acts as a widely expressed promiscuous chemokine receptor and as the erythrocyte receptor for Plasmodium vivax. To gain insight into the evolution and structure/function relations of DARC, we analyzed the binding of anti-human Fy monoclonal antibodies (mAbs) and human chemokines to red blood cells (RBCs) from 11 nonhuman primates and two nonprimate mammals, and we elucidated the structures of the DARC genes from gorilla, gibbon, baboon, marmoset, tamarin, night monkey and cattle. CXCL-8 and CCL-5 chemokine binding analysis indicated that the promiscuous binding profile characteristic of DARC is conserved across species. Among three mAbs that detected the Fy6 epitope by flow cytometric analysis of human and chimpanzee RBCs, only one reacted with night monkey and squirrel monkey. Only chimpanzee RBCs bound a significant amount of the anti-Fy3 mAb. Fy3 was also poorly detected on RBCs from gorilla, baboon and rhesus monkey, but not from new world monkeys. Alignment of DARC homologous sequences allowed us to construct a phylogenetic tree in which all branchings were in accordance with current knowledge of primate phylogeny. Although DARC was expected to be under strong internal and external selection pressure, in order to maintain chemokine binding and avoid Plasmodium vivax binding, respectively, our present study did not provide arguments in favor of a selection pressure on the extracellular domains involved in ligand specificity. The amino acid variability of DARC-like polypeptides was found to be well correlated with the hydrophylicity indexes, with the highest divergence on the amino-terminal extracellular domain. Analysis of the deduced amino acid sequences highlighted the conservation of some amino acid residues, which should prove to be critical for the structural and functional properties of DARC.en
dc.description.affiliationInst Natl Transfus Sanguine, INSERM, U76, F-75015 Paris, France
dc.description.affiliationUniv Toulouse 3, Hop Rangueil, Lab Immunol Mol, F-31059 Toulouse, France
dc.description.affiliationUniv Estadual Paulista, Botucatu, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Botucatu, SP, Brazil
dc.format.extent682-694
dc.identifierhttp://dx.doi.org/10.1007/s00251-003-0633-2
dc.identifier.citationImmunogenetics. New York: Springer-verlag, v. 55, n. 10, p. 682-694, 2004.
dc.identifier.doi10.1007/s00251-003-0633-2
dc.identifier.issn0093-7711
dc.identifier.urihttp://hdl.handle.net/11449/37121
dc.identifier.wosWOS:000188385600004
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofImmunogenetics
dc.relation.ispartofjcr2.094
dc.relation.ispartofsjr0,916
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectDuffy blood group systempt
dc.subjectchemokine receptorpt
dc.subjectphylogenesispt
dc.subjectDARC genespt
dc.subjectnonhuman primatespt
dc.titleSequence, evolution and ligand binding properties of mammalian Duffy antigen/receptor for chemokinesen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer

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