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Antimicrobial Agents and Chemotherapy, Aug 1995, 1871-1874, Vol 39, No. 8
Copyright © 1995 by the American Society for Microbiology. All rights reserved.

Cloning and characterization of the Pseudomonas aeruginosa pbpB gene encoding penicillin-binding protein 3

X Liao and RE Hancock
Department of Microbiology & Immunology, University of British Columbia, Vancouver, Canada.

Clones containing the pbpB gene which encodes penicillin-binding protein (PBP) 3 of Pseudomonas aeruginosa were detected by hybridization by PCR amplification with primers based on the conserved sequences of high-molecular-weight PBPs. The translated amino acid sequence demonstrated 45% identity and had a total of 66% conserved amino acids relative to the Escherichia coli PBP3. The pbpB gene was located upstream of a gene homologous to the E. coli murE gene, which encodes uridine diphosphate-N-acetyl muramic acid-tripeptide synthetase. The overexpressed pbpB gene product reacted with 3H- penicillin G and had an apparent molecular weight of 60,000.


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