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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1985-10-9
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pubmed:abstractText |
A penicillin-susceptible gonococcus and its low-level resistant penA transformant were examined with regard to their penicillin-binding proteins (PBPs) and their peptidoglycan structures. Treatment of the susceptible strain with its MIC of penicillin (0.01 microgram/ml) led to significant binding to PBPs 2 and 3 and a substantial decrease in the O-acetyl modification on the peptidoglycan. Peptidoglycan synthesis gradually ceased over an extended time. When the penA strain was treated with the same concentration of penicillin, only binding to PBP 3 was observed and there was no O-acetylation decrease, with continued peptidoglycan synthesis. This suggested that PBP 2 was the primary target in penicillin-susceptible gonococci and that this protein participated in the O-acetylation of peptidoglycan. Penicillin concentrations representing the MIC for the penA transformant (0.06 microgram/ml) caused significant binding to PBPs 1, 2, and 3 in the susceptible strain and PBPs 1 and 3 in the penA strain. In both strains the rate of peptidoglycan synthesis and the cross-linkage of the peptidoglycan made declined sharply, suggesting that significant inhibition of PBP 1 interfered with transpeptidation. A model for low-level resistance is proposed in which a decreased PBP 2 affinity leads to assumption of the role of primary target in the resistant transformant by PBP 1. The differences observed in peptidoglycan metabolism are a direct consequence of this change.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-122527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-20406,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-221218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-415006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6351730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6352855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6401284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6409990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6417014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6771365,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6776063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6778384,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6790518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-6792979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-810479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-810480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3929684-810484
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0066-4804
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
90-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3929684-Acetylation,
pubmed-meshheading:3929684-Anti-Bacterial Agents,
pubmed-meshheading:3929684-Bacterial Proteins,
pubmed-meshheading:3929684-Carrier Proteins,
pubmed-meshheading:3929684-Hexosyltransferases,
pubmed-meshheading:3929684-Kinetics,
pubmed-meshheading:3929684-Muramoylpentapeptide Carboxypeptidase,
pubmed-meshheading:3929684-Neisseria gonorrhoeae,
pubmed-meshheading:3929684-Penicillin G,
pubmed-meshheading:3929684-Penicillin Resistance,
pubmed-meshheading:3929684-Penicillin-Binding Proteins,
pubmed-meshheading:3929684-Penicillins,
pubmed-meshheading:3929684-Peptidoglycan,
pubmed-meshheading:3929684-Peptidyl Transferases,
pubmed-meshheading:3929684-Structure-Activity Relationship,
pubmed-meshheading:3929684-Transformation, Bacterial
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pubmed:year |
1985
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pubmed:articleTitle |
Involvement of a change in penicillin target and peptidoglycan structure in low-level resistance to beta-lactam antibiotics in Neisseria gonorrhoeae.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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