CHARACTERIZATION OF A 38-KDA PENICILLIN-BINDING PROTEIN AND ITS POSSIBLE INVOLVEMENT IN MAINTAINING STATIONARY-PHASE CELLS OF SHIGELLA-DYSENTERIAE

This paper reports the first attempt to characterize the penicillin-bi nding proteins (PBPs) of Shigella dysenteriae, an important human path ogen. The PBP pattern of the membranes of S. dysenteriae closely resem bles that of Escherichia coli membranes. A 38 kDa PBP which is an impo rtant target for the penem SCH34343, the cephamycin cefoxitin and the oxacephem moxalactam, has been purified. This PBP is immunologically r elated to a PBP of similar molecular mass in E. coli and is present at high levels in stationary-phase cells of S. dysenteriae.