Interactions of Yersinia pestis penicillin-binding proteins with beta-lactam antibiotics

Author:

Ferreira R C1,Park J T1,Camelo D1,De Almeida D F1,Ferreira L C1

Affiliation:

1. Instituto de Biofisica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro-CCS, Brazil.

Abstract

The affinities of six major penicillin-binding proteins (PBPs) of Yersinia pestis EV76 to different beta-lactam antibiotics were determined. The results indicate that, similar to their counterparts in Escherichia coli, PBP2 and PBP3 are the lethal targets of amdinocillin and furazlocillin, respectively. The PBP contents of four additional Y. pestis strains and the morphological effects produced by some beta-lactam antibiotics are also reported.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference15 articles.

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2. Barnes A. M. and T. J. Quan. 1992. Plague p. 1285-1291. In S. L. Gorbach J. G. Bartlett and N. R. Blacklow (ed.) Infectious diseases. The W. B. Saunders Co. Philadelphia.

3. Assessment of a fluoroquinolone, three ~-lactams, two aminoglycosides, and a cycline in treatment of murine Yersinia pestis infection;Bonacorsi S. P.;Antimicrob. Agents Chemother.,1994

4. Plasmid regulation and temperature-sensitive behavior of the Yersinia pestis penicillin-binding proteins;Ferreira R. C. C.;Infect. Immun.,1994

5. Penicillin-binding proteins in bacteria;Georgopapadakou N. H.;Antimicrob. Agents Chemother.,1980

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