ACT-6, a novel plasmid-encoded class C β-lactamase in a Klebsiella pneumoniae isolate from China.
J Antibiot (Tokyo), 2011/4;64(4):317-20.
Zhu YL[1], Zhang XN, Gao F, Cheng J, Hu LF, Ma T, Yin J, Ye Y, Li JB
Affiliations
PMID: 21304534DOI: 10.1038/ja.2011.1
Impact factor: 3.424
Abstract
The purpose of this study was to investigate the phenotypic and molecular characterization of a novel plasmid-mediated AmpC-type β-lactamase in Klebsiella pneumoniae E701 isolated from Anhui province in China. In comparison with the ACT-1, sequence analysis revealed that there were 43 point mutations in the coding gene, and 10 of which led to amino-acid substitution. Resistance could be transferred by conjugation or transformation with plasmid DNA into E. coli JM109, which was due to the production of a β-lactamase with an isoelectric point of 8.4 named ACT-6. Cloning, expression, purification and kinetics were carried out to study the characterization of the novel AmpC-type β-lactamase. The results of MIC determinations and substrate profiles showed there was no significant difference in the activities of the novel enzyme and ACT-1. Moreover, the class 1 integron and the whole open reading frame of the novel AmpC-type β-lactamase from K.pneumoniae E701 were detectable in the same size plasmid. This is the first report on the emergence of the novel ACT-6 type β-lactamases in K. pneumoniae.
MeSH terms
Aged; Amino Acid Sequence; Amino Acid Substitution; Anti-Bacterial Agents; Bacterial Proteins; Base Sequence; China; Drug Resistance, Bacterial; Humans; Isoelectric Point; Klebsiella Infections; Klebsiella pneumoniae; Male; Microbial Sensitivity Tests; Molecular Sequence Data; Open Reading Frames; Plasmids; Point Mutation; Sequence Analysis, DNA; beta-Lactamases
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