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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 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 blaVIM-60 was intI1-blaVIM-60-aadA1-aacA31-qacEdeltaI-sulI on the chromosome. ...[more]

PMID: 30962328

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