The penicillin-binding proteins of 11 pathogenic Escherichia coil stra
ins, including enteropathogenic, enterotoxigenic, enteroinvasive, ente
roaggregative, and enterohemorrhagic E. coli, were detected in gels fo
llowing the labeling oi isolated cell envelopes with [H-3]benzylpenici
llin. The electrophoretic profiles, sensitivities to and morphological
changes induced by beta-lactam antibiotics showed that the penicillin
-binding proteins of most pathogenic E. coli possess structural and ph
ysiological functions similar to those of E. coil K12. (C) 1998 Publis
hed by Elsevier Science B.V. All rights reserved.