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IMP-51, a novel IMP-type metallo-ß-lactamase with increased doripenem- and meropenem-hydrolyzing activities, in a carbapenem-resistant Pseudomonas aeruginosa clinical isolate.
Tada, Tatsuya; Nhung, Pham Hong; Miyoshi-Akiyama, Tohru; Shimada, Kayo; Phuong, Doan Mai; Anh, Nguyen Quoc; Ohmagari, Norio; Kirikae, Teruo.
Afiliação
  • Tada T; Department of Infectious Diseases, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan.
  • Nhung PH; Department of Microbiology, Hanoi Medical University, Hanoi, Vietnam Bach Mai Hospital, Hanoi, Vietnam.
  • Miyoshi-Akiyama T; Pathogenic Microbe Laboratory, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan.
  • Shimada K; Department of Infectious Diseases, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan.
  • Phuong DM; Bach Mai Hospital, Hanoi, Vietnam.
  • Anh NQ; Bach Mai Hospital, Hanoi, Vietnam.
  • Ohmagari N; Disease Control and Prevention Center, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan.
  • Kirikae T; Department of Infectious Diseases, Research Institute, National Center for Global Health and Medicine, Tokyo, Japan tkirikae@ri.ncgm.go.jp.
Antimicrob Agents Chemother ; 59(11): 7090-3, 2015 Nov.
Article em En | MEDLINE | ID: mdl-26282421
ABSTRACT
A meropenem-resistant Pseudomonas aeruginosa isolate was obtained from a patient in a medical setting in Hanoi, Vietnam. The isolate was found to have a novel IMP-type metallo-ß-lactamase, IMP-51, which differed from IMP-7 by an amino acid substitution (Ser262Gly). Escherichia coli expressing blaIMP-51 showed greater resistance to cefoxitin, meropenem, and moxalactam than E. coli expressing blaIMP-7. The amino acid residue at position 262 was located near the active site, proximal to the H263 Zn(II) ligand.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pseudomonas aeruginosa / Beta-Lactamases / Carbapenêmicos / Tienamicinas Idioma: En Ano de publicação: 2015 Tipo de documento: Article
Texto completo
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XML
PubMed Links
Buscar no Google

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Pseudomonas aeruginosa / Beta-Lactamases / Carbapenêmicos / Tienamicinas Idioma: En Ano de publicação: 2015 Tipo de documento: Article