rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5310
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pubmed:dateCreated |
1997-4-28
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pubmed:abstractText |
Bacterial pathogenesis requires proteins that sense host microenvironments and respond by regulating virulence gene transcription. For Salmonellae, one such regulatory system is PhoP-PhoQ, which regulates genes required for intracellular survival and resistance to cationic peptides. Analysis by mass spectrometry revealed that Salmonella typhimurium PhoP-PhoQ regulated structural modifications of lipid A, the host signaling portion of lipopolysaccharide (LPS), by the addition of aminoarabinose and 2-hydroxymyristate. Structurally modified lipid A altered LPS-mediated expression of the adhesion molecule E-selectin by endothelial cells and tumor necrosis factor-alpha expression by adherent monocytes. Thus, altered responses to environmentally induced lipid A structural modifications may represent a mechanism for bacteria to gain advantage within host tissues.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabinose,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/E-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid A,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/PhoP protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/PhoQ protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/aminoarabinose
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0036-8075
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
11
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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 |
250-3
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9092473-Acylation,
pubmed-meshheading:9092473-Arabinose,
pubmed-meshheading:9092473-Bacterial Proteins,
pubmed-meshheading:9092473-E-Selectin,
pubmed-meshheading:9092473-Endothelium, Vascular,
pubmed-meshheading:9092473-Fatty Acids,
pubmed-meshheading:9092473-Genes, Bacterial,
pubmed-meshheading:9092473-Humans,
pubmed-meshheading:9092473-Lipid A,
pubmed-meshheading:9092473-Lipopolysaccharides,
pubmed-meshheading:9092473-Monocytes,
pubmed-meshheading:9092473-Salmonella typhimurium,
pubmed-meshheading:9092473-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:9092473-Tumor Necrosis Factor-alpha,
pubmed-meshheading:9092473-Virulence
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pubmed:year |
1997
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pubmed:articleTitle |
Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ.
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pubmed:affiliation |
Department of Medicine, University of Washington, Seattle, WA 98195, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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