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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2004-3-5
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pubmed:abstractText |
Penicillin-binding proteins (PBPs) mediate susceptibility to beta-lactam antibiotics. PBP 4, although not essential for survival, has been associated with low-level resistance to beta-lactam antibiotics. To determine its contribution to survival of Staphylococcus aureus cells exposed to beta-lactams, the PBP 4 gene (pbp4) was disrupted and then complemented in the methicillin-susceptible strain RN4220 and the homogeneous methicillin-resistant strain COL. Depending on the antibiotic tested, the presence or absence of an intact pbp4 has no effect or only a modest effect on growth measured by population analysis. These data indicate that PBP 4 is a relatively unimportant target of beta-lactams not only in methicillin-susceptible but also methicillin-resistant S. aureus.
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pubmed:grant |
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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/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide...,
http://linkedlifedata.com/resource/pubmed/chemical/Nafcillin,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Penicillins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases
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pubmed:status |
MEDLINE
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pubmed:issn |
1076-6294
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
329-36
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15000739-Anti-Bacterial Agents,
pubmed-meshheading:15000739-Bacterial Proteins,
pubmed-meshheading:15000739-Carrier Proteins,
pubmed-meshheading:15000739-DNA, Bacterial,
pubmed-meshheading:15000739-Electroporation,
pubmed-meshheading:15000739-Genes, Bacterial,
pubmed-meshheading:15000739-Genetic Complementation Test,
pubmed-meshheading:15000739-Hexosyltransferases,
pubmed-meshheading:15000739-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:15000739-Mutagenesis,
pubmed-meshheading:15000739-Nafcillin,
pubmed-meshheading:15000739-Penicillin-Binding Proteins,
pubmed-meshheading:15000739-Penicillins,
pubmed-meshheading:15000739-Peptidyl Transferases,
pubmed-meshheading:15000739-Plasmids,
pubmed-meshheading:15000739-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15000739-Staphylococcus aureus,
pubmed-meshheading:15000739-beta-Lactam Resistance
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pubmed:year |
2003
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pubmed:articleTitle |
Effect of disruption of Staphylococcus aureus PBP4 gene on resistance to beta-lactam antibiotics.
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pubmed:affiliation |
Division of Infectious Diseases, San Francisco General Hospital, Department of Medicine, University of California San Francisco, San Francisco, CA 94110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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