Penicillin-binding proteins and induction of AmpC beta-lactamase
Author(s) -
Christine C. Sanders,
Patricia A. Bradford,
Anton F. Ehrhardt,
Karen Bush,
Kevin D. Young,
Thomas A. Henderson,
William E. Sanders
Publication year - 1997
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.41.9.2013
Subject(s) - penicillin binding proteins , penicillin , microbiology and biotechnology , beta lactamase inhibitors , beta lactamase , antibiotics , chemistry , biology , biochemistry , escherichia coli , gene
In competition assays for radiolabeled penicillin, penicillin-binding proteins (PBPs) 4, 7a, and 7b showed very high affinities for strong inducers of AmpC beta-lactamase. Loss of PBP 4 resulted in diminished inducibility. This suggests that if PBPs are involved in induction of AmpC beta-lactamase, there is probably a redundancy in function among the different PBPs.
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