PENICILLIN-BINDING PROTEINS OF PATHOGENIC YERSINIA SPECIES

The penicillin-binding proteins (PBPs) of Yersinia pestis, I: enteroco litica and Y. pseudotuberculosis grown at 28 degrees C or 37 degrees C were detected after labeling with [H-3]-benzylpenicillin and fluorogr aphy of polyacrylamide gels. Each sample showed a unique PBP profile c omposed of three to six proteins, with molecular weights ranging from 120,000 to 43,000. Incubation at 37 degrees C resulted in significant changes of the PBP profiles of all three species. The possible implica tions of these results on the physiology of these bacteria and on the action of beta-lactam antibiotics are discussed.