English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/3620
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
DC FieldValueLanguage
dc.contributor.authorFrade, José M.R.-
dc.contributor.authorLlorente Gómez, María de las Mercedes-
dc.contributor.authorMellado, Mario-
dc.contributor.authorAlcamí, José-
dc.contributor.authorGutiérrez Ramos, José Carlos-
dc.contributor.authorZaballos, Ángel-
dc.contributor.authorReal, Gustavo del-
dc.contributor.authorMartínez-Alonso, Carlos-
dc.identifier.citationThe Journal of Clinical Investigation, vol. 100(3), pp. 497-502, (1997)en_US
dc.description.abstractThe chemokines are a homologous serum protein family characterized by their ability to induce activation of integrin adhesion molecules and leukocyte migration. Chemokines interact with their receptors, which are composed of a single-chain, seven-helix, membrane-spanning protein coupled to G proteins. Two CC chemokine receptors, CCR3 and CCR5, as well as the CXCR4 chemokine receptor, have been shown necessary for infection by several HIV-1 virus isolates. We studied the effect of the chemokine monocyte chemoattractant protein 1 (MCP-1) and of a panel of MCP-1 receptor (CCR2)-specific monoclonal antibodies (mAb) on the suppression of HIV-1 replication in peripheral blood mononuclear cells. We have compelling evidence that MCP-1 has potent HIV-1 suppressive activity when HIV-1–infected peripheral blood lymphocytes are used as target cells. Furthermore, mAb specific for the MCP-1R CCR2 which recognize the third extracellular CCR2 domain inhibit all MCP-1 activity and also block MCP-1 suppressive activity. Finally, a set of mAb specific for the CCR2 amino-terminal domain, one of which mimics MCP-1 activity, has a potent suppressive effect on HIV-1 replication in M- and T-tropic HIV-1 viral isolates. We conjecture a role for CCR2 as a coreceptor for HIV-1 infection and map the HIV-1 binding site to the amino-terminal part of this receptor. This concurs with results showing that the CCR5 amino terminus is relevant in HIV-1 infection, although chimeric fusion of various extracellular domains shows that other domains are also implicated. We discuss the importance of CCR2 structure relative to its coreceptor role and the role of anti-CCR2 receptor antibodies in the prevention of HIV-1 infection.en_US
dc.format.extent204291 bytes-
dc.publisherAmerican Society for Clinical Investigationen_US
dc.subjectChemokine receptoren_US
dc.subjectHIV-1 coreceptoren_US
dc.subjectMonoclonal antibodiesen_US
dc.titleThe amino-terminal domain of the CCR2 chemokine receptor acts as coreceptor for HIV-1 infectionen_US
dc.description.peerreviewedPeer revieweden_US
Appears in Collections:(CNB) Artículos
Files in This Item:
File Description SizeFormat 
211.pdf199,5 kBAdobe PDFThumbnail
Show simple item record

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.