pubmed-article:20542250 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20542250 | lifeskim:mentions | umls-concept:C0038172 | lld:lifeskim |
pubmed-article:20542250 | lifeskim:mentions | umls-concept:C0537254 | lld:lifeskim |
pubmed-article:20542250 | lifeskim:mentions | umls-concept:C0205250 | lld:lifeskim |
pubmed-article:20542250 | lifeskim:mentions | umls-concept:C0450254 | lld:lifeskim |
pubmed-article:20542250 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:20542250 | pubmed:dateCreated | 2010-6-14 | lld:pubmed |
pubmed-article:20542250 | pubmed:abstractText | Virulence of emerging community-associated methicillin-resistant Staphylococcus aureus (CA-MRSA) and other highly pathogenic S. aureus strains depends on their production of phenol-soluble modulin (PSM) peptide toxins, which combine the capacities to attract and lyse neutrophils. The molecular basis of PSM-stimulated neutrophil recruitment has remained unclear. Here, we demonstrate that the human formyl peptide receptor 2 (FPR2/ALX), which has previously been implicated in control of endogenous inflammatory processes, senses PSMs at nanomolar concentrations and initiates proinflammatory neutrophil responses to CA-MRSA. Specific blocking of FPR2/ALX or deletion of PSM genes in CA-MRSA severely diminished neutrophil detection of CA-MRSA. Furthermore, a specific inhibitor of FPR2/ALX and of its functional mouse counterpart blocked PSM-mediated leukocyte infiltration in vivo in a mouse model. Thus, the innate immune system uses a distinct FPR2/ALX-dependent mechanism to specifically sense bacterial peptide toxins and detect highly virulent bacterial pathogens. FPR2/ALX represents an attractive target for new anti-infective or anti-inflammatory strategies. | lld:pubmed |
pubmed-article:20542250 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:language | eng | lld:pubmed |
pubmed-article:20542250 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20542250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20542250 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20542250 | pubmed:month | Jun | lld:pubmed |
pubmed-article:20542250 | pubmed:issn | 1934-6069 | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:SchönebergTor... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:WangRongR | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:PeschelAndrea... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:OttoMichaelM | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:BoulayFrancoi... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:BohnErwinE | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:van... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:GleskeAnne-Ka... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:KlebanoffSeym... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:KöberleMartin... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:KretschmerDor... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:RabietMarie-J... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:RautenbergMar... | lld:pubmed |
pubmed-article:20542250 | pubmed:author | pubmed-author:van... | lld:pubmed |
pubmed-article:20542250 | pubmed:copyrightInfo | Copyright (c) 2010 Elsevier Inc. All rights reserved. | lld:pubmed |
pubmed-article:20542250 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20542250 | pubmed:day | 25 | lld:pubmed |
pubmed-article:20542250 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:20542250 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20542250 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20542250 | pubmed:pagination | 463-73 | lld:pubmed |
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pubmed-article:20542250 | pubmed:meshHeading | pubmed-meshheading:20542250... | lld:pubmed |
pubmed-article:20542250 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20542250 | pubmed:articleTitle | Human formyl peptide receptor 2 senses highly pathogenic Staphylococcus aureus. | lld:pubmed |
pubmed-article:20542250 | pubmed:affiliation | Cellular and Molecular Microbiology Division, Interfaculty Institute of Microbiology and Infection Medicine, University of Tübingen, Elfriede-Aulhorn-Strasse 6, 72076 Tübingen, Germany. | lld:pubmed |
pubmed-article:20542250 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20542250 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:20542250 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
entrez-gene:2358 | entrezgene:pubmed | pubmed-article:20542250 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20542250 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:20542250 | lld:pubmed |