Penicillin-binding proteins of pathogenic Escherichia coli strains.
The penicillin-binding proteins of 11 pathogenic Escherichia coli strains, including enteropathogenic, enterotoxigenic, enteroinvasive, enteroaggregative, and enterohemorrhagic E. coli, were detected in gels following the labeling of isolated cell envelopes with [3H]benzylpenicillin. The electrophoretic profiles, sensitivities to and morphological changes induced by beta-lactam antibiotics showed that the penicillin-binding proteins of most pathogenic E. coli possess structural and physiological functions similar to those of E. coli K12.
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Departamento de Microbiologia, Universidade de São Paulo, Brazil. ritacafe@usp.br
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Trabulsi
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D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D003967:Diarrhea / Q000382:microbiology*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry* / Q000145:classification / Q000187:drug effects / Q000378:metabolism; D004927:Escherichia coli Infections / Q000382:microbiology*; D006602:Hexosyltransferases; D006801:Humans; D007769:Lactams; D008826:Microbial Sensitivity Tests; D002267:Muramoylpentapeptide Carboxypeptidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D012703:Serotyping
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase