A novel type of AmpC beta-lactamase, ACC-1, produced by a Klebsiella pneumoniae strain causing nosocomial pneumonia.
Antimicrob Agents Chemother, 1999/8;43(8):1924-31.
Bauernfeind A[1], Schneider I, Jungwirth R, Sahly H, Ullmann U
Affiliations
PMID: 10428914
Impact factor: 5.938
Abstract
A Klebsiella pneumoniae strain resistant to oxyimino cephalosporins was cultured from respiratory secretions of a patient suffering from nosocomial pneumonia in Kiel, Germany, in 1997. The isolate harbors a bla resistance gene located on a transmissible plasmid. An Escherichia coli transconjugant produces a beta-lactamase with an isoelectric point of 7.7 and a resistance phenotype characteristic of an AmpC (class 1) beta-lactamase except for low MICs of cephamycins. The bla gene was cloned and sequenced. It encodes a protein of 386 amino acids with the active site serine of the S-X-X-K motif at position 64, as is characteristic for class C beta-lactamases. Multiple alignment of the deduced amino acid sequence with 21 other AmpC beta-lactamases demonstrates only very distant homology, reaching at maximum 52.3% identity for the chromosomal AmpC beta-lactamase of Serratia marcescens SR50. The beta-lactamase of K. pneumoniae KUS represents a new type of AmpC-class enzyme, for which we propose the designation ACC-1 (Ambler class C-1).
MeSH terms
Adult; Amino Acid Sequence; Bacterial Proteins; Base Sequence; Cloning, Molecular; Cross Infection; Humans; Isoelectric Focusing; Kinetics; Klebsiella Infections; Klebsiella pneumoniae; Male; Microbial Sensitivity Tests; Molecular Sequence Data; Phenotype; Pneumonia, Bacterial; Sequence Homology, Amino Acid; beta-Lactamases
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