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A Novel VIM-Type Metallo-?-Lactamase Variant, VIM-60, with Increased Hydrolyzing Activity against Fourth-Generation Cephalosporins in Pseudomonas aeruginosa Clinical Isolates in Japan.


ABSTRACT: A novel VIM-type metallo-?-lactamase variant, VIM-60, was identified in multidrug-resistant Pseudomonas aeruginosa clinical isolates in Japan. Compared with VIM-2, VIM-60 had two amino acid substitutions (Arg228Leu and His252Arg) and higher catalytic activities against fourth-generation cephalosporins. The genetic context for bla VIM-60 was intI1-bla VIM-60-aadA1-aacA31-qacEdeltaI-sulI on the chromosome.

SUBMITTER: Hishinuma T 

PROVIDER: S-EPMC6535569 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

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A Novel VIM-Type Metallo-β-Lactamase Variant, VIM-60, with Increased Hydrolyzing Activity against Fourth-Generation Cephalosporins in Pseudomonas aeruginosa Clinical Isolates in Japan.

Hishinuma Tomomi T   Tada Tatsuya T   Uchida Hiroki H   Shimojima Masahiro M   Kirikae Teruo T  

Antimicrobial agents and chemotherapy 20190524 6


A novel VIM-type metallo-β-lactamase variant, VIM-60, was identified in multidrug-resistant <i>Pseudomonas aeruginosa</i> clinical isolates in Japan. Compared with VIM-2, VIM-60 had two amino acid substitutions (Arg228Leu and His252Arg) and higher catalytic activities against fourth-generation cephalosporins. The genetic context for <i>bla</i><sub>VIM-60</sub> was <i>intI1-bla</i><sub>VIM-60</sub>-<i>aadA1-aacA31-qacEdeltaI-sulI</i> on the chromosome. ...[more]

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