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This paper reports the first attempt to characterize the penicillin-binding proteins (PBPs) of Shigella dysenteriae,an important human pathogen. The PBP pattern of the membranes of S. dysenteriaeclosely resembles that of Escherichia colimembranes. A 38 kDa PBP which is an important target for the penem SCH34343, the cephamycin cefoxitin and the oxacephem moxalactam, has been purified. This PBP is immunologically related to a PBP of similar molecular mass in E. coliand is present at high levels in stationary-phase cells of S. dysenteriae.
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