Activity of cefixime against Helicobacter pylori and affinities for the penicillin-binding proteins.
Cefixime induced the formation of rounded cells from the spiral bacillary form of Helicobacter pylori at the MIC or less. Three main penicillin-binding proteins, called A, B and C, were separated from H. pylori. Cefixime had the strongest affinity to penicillin-binding protein B. The binding of cefixime to this protein may induce the formation of rounded H. pylori cells.
Ikeda
F
F
Department of Chemotherapy, Fujisawa Pharmaceutical Co., Ltd., Osaka, Japan.
Yokota
Y
Y
Mine
Y
Y
Tatsuta
M
M
D000892:Anti-Infective Agents, Urinary / Q000378:metabolism / Q000494:pharmacology*; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism*; D020682:Cefixime; D002439:Cefotaxime / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D003470:Culture Media; D004926:Escherichia coli / Q000187:drug effects / Q000648:ultrastructure; D016480:Helicobacter pylori / Q000187:drug effects*; D006602:Hexosyltransferases; D008855:Microscopy, Electron, Scanning; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases
D000892:Anti-Infective Agents, Urinary; D001426:Bacterial Proteins; D002352:Carrier Proteins; D003470:Culture Media; D046915:Penicillin-Binding Proteins; D020682:Cefixime; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D002439:Cefotaxime