The bacteriolytic action of MT-141, a new cephamycin antibiotic, on gram-negative bacteria.
MT-141, a new cephamycin (7 alpha-methoxy-cephalosporin) antibiotic with a D-cysteine moiety in its 7 beta-side chain, has binding affinities to penicillin-binding proteins of Escherichia coli and an inhibitory action on their transpeptidase activity similar to those of other structurally related cephamycins. Yet this antibiotic was found to exert an exceedingly strong and rapid lytic action on sensitive Gram-negative bacteria such as E. coli, Klebsiella pneumoniae, Serratia marcescens and Salmonella enteritidis. Not only rapidly growing cells, but also slowly growing dense cells of the above bacteria could be lysed by this antibiotic at low concentrations. In the presence of 20% sucrose, low concentrations of MT-141 induced smooth-surfaced single and twin bulges of the putative growth zone of the cells and irregularly orientated rough-surfaced bulges. Probably the 7 beta-side chain structure of this antibiotic is involved in its rapid and strong bacteriolytic action.
D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism; D002513:Cephamycins / Q000494:pharmacology*; D003470:Culture Media; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology; D006090:Gram-Negative Bacteria / Q000187:drug effects* / Q000648:ultrastructure; D006602:Hexosyltransferases; D008826:Microbial Sensitivity Tests; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism; D010400:Penicillin G / Q000494:pharmacology; D010403:Penicillin Resistance; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases / Q000378:metabolism; D013997:Time Factors
D001426:Bacterial Proteins; D002352:Carrier Proteins; D002513:Cephamycins; D003470:Culture Media; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; C046079:cefminox; D010400:Penicillin G