Source:http://linkedlifedata.com/resource/pubmed/id/15225317
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-6-30
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pubmed:abstractText |
In Salmonella enterica, the PhoP-PhoQ two-component system governs resistance to structurally different antimicrobial peptides including the alpha-helical magainin 2, the beta-sheet defensins and the cyclic lipopeptide polymyxin B. To identify the PhoP-regulated determinants mediating peptide resistance, we prepared a plasmid library from a phoP mutant, introduced it into a phoP mutant and selected for magainin-resistant clones. One of the clones harboured the PhoP-activated ugtL gene, deletion of which rendered Salmonella susceptible to magainin 2 and polymyxin B, but not defensin HNP-1. We established that ugtL encodes an inner membrane protein that promotes the formation of monophosphorylated lipid A in the lipopolysaccharide. Inactivation of both ugtL and the regulatory gene pmrA, which controls lipid A modifications required for resistance to polymxyin B (but not to magainin 2) and is post-transcriptionally activated by the PhoP-PhoQ system, resulted in a strain that was as susceptible to polymyxin B as a phoP mutant. The most frequently recovered clone harboured the yqjA gene, which we show is PhoP regulated and required for resistance to magainin 2 but not to polymyxin B or defensin HNP-1. Our results indicate that different PhoP-mediated modifications in lipid A are necessary for resistance to different antimicrobial peptides.
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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/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/PhoP protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Polymyxins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0950-382X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
229-41
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15225317-Anti-Bacterial Agents,
pubmed-meshheading:15225317-Bacterial Proteins,
pubmed-meshheading:15225317-Drug Resistance, Bacterial,
pubmed-meshheading:15225317-Gene Expression Regulation, Bacterial,
pubmed-meshheading:15225317-Genes, Bacterial,
pubmed-meshheading:15225317-Microbial Sensitivity Tests,
pubmed-meshheading:15225317-Peptides,
pubmed-meshheading:15225317-Polymyxins,
pubmed-meshheading:15225317-Salmonella,
pubmed-meshheading:15225317-Transcriptional Activation
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pubmed:year |
2004
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pubmed:articleTitle |
PhoP-regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B.
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pubmed:affiliation |
Department of Molecular Microbiology, Campus Box 8230, Washington University, St Louis, MO 63110, 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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