Penicillin-binding proteins in Clostridium perfringens.

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Murphy TF, Barza M, Park JT

Penicillin-binding proteins in Clostridium perfringens.

Antimicrob Agents Chemother. 1981 Dec;20(6):809-13. doi: 10.1128/aac.20.6.809.

PubMed ID

6275787 [ View in PubMed

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Abstract

The penicillin-binding proteins (PBPs) of Clostridium perfringens were studied. Six PBPs ranging in molecular weight from approximately 42,000 to 100,000 were detected in the cytoplasmic membrane. The relative affinities of the PBPs for 16 beta-lactam antibiotics were determined. Most of the drug saturated PBP 3 and 4 at concentrations equal to their minimal inhibitory concentrations, suggesting that these PBPs are the killing targets for beta-lactams. Mecillinam showed unique properties; it had a higher affinity for PBP 5 than for other PBPs, and it was the only agent tested which caused inhibition of growth without saturating PBP 4. Interestingly, all beta-lactam antibiotics tested induced filament formation despite having different binding patterns to the PBPs of C. perfringens.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Cyclacillin	Penicillin-binding protein (Protein Group)	Protein group	Gram positive and gram negative bacteria	Yes	Inhibitor	Details
Phenoxymethylpenicillin	Penicillin-binding protein 1A	Protein	Clostridium perfringens (strain 13 / Type A)	Yes	Not Available	Details