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Characterization of a 38 kDa penicillin-binding protein and its possible involvement in maintaining stationary-phase cells of Shigella dysenteriae

¹Department of Chemistry, Bose Institute, 93/1 APC Road, Calcutta 700 009, India
²Laboratorium voor Microbiologie, Rijksuniversiteit-Gent, K. L. Ledeganckstraat 35, B-9000 Gent, Belgium

Author for correspondence: Manikuntala Kundu. Fax: +91 33 350 6790.

ABSTRACT

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. dysenteriae closely resembles that of Escherichia coli membranes. 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. coli and is present at high levels in stationary-phase cells of S. dysenteriae.

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