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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
2005-6-23
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pubmed:abstractText |
The attachment protein (glycoprotein) of respiratory syncytial virus (RSV) has long been associated with disease potentiation and respiratory symptoms. The glycoprotein has a conserved cysteine-rich region (GCRR) whose function is unknown and which is not necessary for efficient viral replication. In this report, we show that the GCRR is a powerful inhibitor of the innate immune response against RSV, and that early secretion of glycoprotein is critical to modulate inflammation after RSV infection. Importantly, the GCRR is also a potent inhibitor of cytokine production mediated by several TLR agonists, indicating that this peptide sequence displays broad antiinflammatory properties. These findings have important implications for RSV pathogenesis and describe an inhibitor of TLR-mediated inflammatory responses that could have clinical applications.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-10846112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-11062499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-11083887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-11477410,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-12239255,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-12404174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-12574374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-12925853,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-14963332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-15141000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-15143473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-15289505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-15322205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-15567433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-2117070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-2441388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-3895437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-7507282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-7551415,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15956195-9568029
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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/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/G protein, Bovine respiratory...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycophorin,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/attachment protein G
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
pubmed-author:CollinsPeter LPL,
pubmed-author:DelgadoM FlorenciaMF,
pubmed-author:HendryR MichaelRM,
pubmed-author:HoffmanScott JSJ,
pubmed-author:IrustaPablo MPM,
pubmed-author:KarronRuth ARA,
pubmed-author:KleebergerSteven RSR,
pubmed-author:LahamFederico RFR,
pubmed-author:MelendiGuillermina AGA,
pubmed-author:MeleroJose AJA,
pubmed-author:PolackFernando PFP,
pubmed-author:SchiattiM PaulaMP,
pubmed-author:ThumarBhagvanjiB
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8996-9001
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15956195-Amino Acid Sequence,
pubmed-meshheading:15956195-Animals,
pubmed-meshheading:15956195-Antigens, CD,
pubmed-meshheading:15956195-Conserved Sequence,
pubmed-meshheading:15956195-Cysteine,
pubmed-meshheading:15956195-Female,
pubmed-meshheading:15956195-Glycophorin,
pubmed-meshheading:15956195-Immunity, Innate,
pubmed-meshheading:15956195-Leukocytes, Mononuclear,
pubmed-meshheading:15956195-Lipopolysaccharides,
pubmed-meshheading:15956195-Mice,
pubmed-meshheading:15956195-Mice, Inbred C57BL,
pubmed-meshheading:15956195-Molecular Sequence Data,
pubmed-meshheading:15956195-NF-kappa B,
pubmed-meshheading:15956195-Peptide Fragments,
pubmed-meshheading:15956195-Respiratory Syncytial Viruses,
pubmed-meshheading:15956195-Viral Envelope Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
The cysteine-rich region of respiratory syncytial virus attachment protein inhibits innate immunity elicited by the virus and endotoxin.
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pubmed:affiliation |
Department of Pediatrics, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA. fpolack@jhsph.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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