Interactions of Yersinia pestis penicillin-binding proteins with beta-lactam antibiotics.
The affinities of six major penicillin-binding proteins (PBPs) of Yersinia pestis EV76 to different beta-lactam antibiotics were determined. The results indicate that, similar to their counterparts in Escherichia coli, PBP2 and PBP3 are the lethal targets of amdinocillin and furazlocillin, respectively. The PBP contents of four additional Y. pestis strains and the morphological effects produced by some beta-lactam antibiotics are also reported.
D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase / Q000737:chemistry / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D011485:Protein Binding; D015010:Yersinia pestis / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D047090:beta-Lactams; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase