Multiple Low-Reactivity Class B Penicillin-Binding Proteins Are Required for Cephalosporin Resistance in Enterococci
Dušanka Djorić, Jaime L. Little, Christopher J. Kristich
Abstract
mutant exhibits a variety of phenotypic defects in growth kinetics, cell wall integrity, and cellular morphology, indicating that PbpA(2b) and Pbp5(4) are not functionally redundant and that PbpA(2b) plays a more central role in peptidoglycan synthesis. Collectively, our results shift the current understanding of enterococcal cephalosporin resistance and suggest a model in which PbpA(2b) and Pbp5(4) cooperate to coordinately mediate peptidoglycan cross-linking in the presence of cephalosporins.
Topics & Concepts
Enterococcus faeciumPenicillin binding proteinsEnterococcus faecalisMicrobiologyCephalosporinEnterococcusAntibioticsPenicillinAntibiotic resistanceBiologyBacteriaStaphylococcus aureusGeneticsAntimicrobial Resistance in StaphylococcusClostridium difficile and Clostridium perfringens researchAntibiotic Resistance in Bacteria