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The amino-terminal domain of the CCR2 chemokine receptor acts as coreceptor for HIV-1 infection

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dc.creator Frade, José M.R.
dc.creator Llorente Gómez, María de las Mercedes
dc.creator Mellado, Mario
dc.creator Alcamí, José
dc.creator Gutiérrez Ramos, José Carlos
dc.creator Zaballos, Ángel
dc.creator Real, Gustavo del
dc.creator Martínez-Alonso, Carlos
dc.date 2008-04-16T11:12:03Z
dc.date 2008-04-16T11:12:03Z
dc.date 1997-08
dc.date.accessioned 2017-01-31T01:02:27Z
dc.date.available 2017-01-31T01:02:27Z
dc.identifier The Journal of Clinical Investigation, vol. 100(3), pp. 497-502, (1997)
dc.identifier 0021-9738
dc.identifier http://hdl.handle.net/10261/3620
dc.identifier 10.1172/JCI119558.
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3620
dc.description The 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.
dc.description Peer reviewed
dc.format 204291 bytes
dc.format application/pdf
dc.language eng
dc.publisher American Society for Clinical Investigation
dc.rights openAccess
dc.subject Chemokine receptor
dc.subject HIV-1 coreceptor
dc.subject Monoclonal antibodies
dc.title The amino-terminal domain of the CCR2 chemokine receptor acts as coreceptor for HIV-1 infection
dc.type Artículo


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