rdf:type |
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lifeskim:mentions |
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pubmed:issue |
46
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pubmed:dateCreated |
2001-11-12
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pubmed:abstractText |
Monocyte chemoattractant protein-1 (MCP-1) is a chemotactic cytokine mainly acting on monocytes and T cells that elicits its biological effects by interacting with the seven-transmembrane helix receptor CCR2B. The vaccinia virus strain Lister and many other poxviruses express soluble proteins (vCCI) that bind MCP-1 and other CC chemokines and inhibit their function. In order to define the interaction site of MCP-1 with vCCI from vaccinia, surface exposed residues of MCP-1 were identified and mutated to alanine. The MCP-1 variants were expressed, purified, and their interaction with vCCI was characterized. The site on MCP-1 for vCCI binding is dominated by arginine 18 with important additional contributions from tyrosine 13 and arginine 24. These residues define a binding site that largely overlaps with the CCR2B receptor interaction site. The viral chemokine-binding protein vCCI thus inhibits the biological function of MCP-1 by directly masking its CCR2B receptor-binding site.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/CCI protein, Cowpox virus,
http://linkedlifedata.com/resource/pubmed/chemical/CCR2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Chemokine CCL2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, CCR2,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Chemokine,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
43270-6
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11551937-Alanine,
pubmed-meshheading:11551937-Animals,
pubmed-meshheading:11551937-Antibodies, Monoclonal,
pubmed-meshheading:11551937-Arginine,
pubmed-meshheading:11551937-Binding Sites,
pubmed-meshheading:11551937-CHO Cells,
pubmed-meshheading:11551937-Calcium,
pubmed-meshheading:11551937-Chemokine CCL2,
pubmed-meshheading:11551937-Cloning, Molecular,
pubmed-meshheading:11551937-Cricetinae,
pubmed-meshheading:11551937-Dose-Response Relationship, Drug,
pubmed-meshheading:11551937-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:11551937-Humans,
pubmed-meshheading:11551937-Kinetics,
pubmed-meshheading:11551937-Models, Molecular,
pubmed-meshheading:11551937-Mutation,
pubmed-meshheading:11551937-Protein Binding,
pubmed-meshheading:11551937-Receptors, CCR2,
pubmed-meshheading:11551937-Receptors, Chemokine,
pubmed-meshheading:11551937-Surface Plasmon Resonance,
pubmed-meshheading:11551937-Two-Hybrid System Techniques,
pubmed-meshheading:11551937-Tyrosine,
pubmed-meshheading:11551937-Viral Proteins,
pubmed-meshheading:11551937-Virulence Factors
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pubmed:year |
2001
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pubmed:articleTitle |
The viral CC chemokine-binding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B-binding site.
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pubmed:affiliation |
Department of Arthritis Biology, Novartis Pharma AG, CH-4002 Basel, Switzerland.
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pubmed:publicationType |
Journal Article
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