• Media type: E-Article
  • Title: IMP-68, a Novel IMP-Type Metallo-β-Lactamase in Imipenem-Susceptible Klebsiella pneumoniae
  • Contributor: Kubota, Hiroaki; Suzuki, Yasunori; Okuno, Rumi; Uchitani, Yumi; Ariyoshi, Tsukasa; Takemura, Nobuyuki; Mihara, Fuminori; Mezaki, Kazuhisa; Ohmagari, Norio; Matsui, Mari; Suzuki, Satowa; Sekizuka, Tsuyoshi; Kuroda, Makoto; Yokoyama, Keiko; Sadamasu, Kenji
  • imprint: American Society for Microbiology, 2019
  • Published in: mSphere
  • Language: English
  • DOI: 10.1128/msphere.00736-19
  • ISSN: 2379-5042
  • Origination:
  • Footnote:
  • Description: <jats:p> IMP-type metallo-β-lactamases comprise one group of the “Big 5” carbapenemases. Here, a novel <jats:italic>bla</jats:italic> <jats:sub>IMP-68</jats:sub> gene encoding IMP-68 (harboring a Ser262Gly point mutant of IMP-11) was discovered from meropenem-resistant but imipenem-susceptible <jats:named-content content-type="genus-species">Klebsiella pneumoniae</jats:named-content> TA6363. The Ser262Gly substitution was previously identified as important for substrate specificity according to a study of other IMP variants, including IMP-6. We confirmed that IMP-68 exhibited weaker imipenem-hydrolyzing activity than that for other carbapenems, demonstrating that the antimicrobial susceptibility profile of TA6363 originated from IMP-68 substrate specificity, with this likely to affect treatment strategies using antibacterial agents in clinical settings. Notably, the carbapenem resistance conferred by IMP-68 was undetectable based on the MIC of imipenem as a carbapenem representative, which demonstrates a comparable antimicrobial susceptibility profile to IMP-6-producing <jats:italic>Enterobacteriaceae</jats:italic> that previously spread in Japan due to lack of awareness of its existence. </jats:p>
  • Access State: Open Access