Characterization of OXA-181, a Carbapenem-Hydrolyzing Class D β-Lactamase from Klebsiella pneumoniae | Zendy

Anaïs Potron | Zendy; Patrice Nordmann | Zendy; Emilie Lafeuille | Zendy; Zaina Al Maskari | Zendy; Fatma Al Rashdi | Zendy; Laurent Poirel | Zendy

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Characterization of OXA-181, a Carbapenem-Hydrolyzing Class D β-Lactamase from Klebsiella pneumoniae

Author(s) -

Anaïs Potron,

Patrice Nordmann,

Emilie Lafeuille,

Zaina Al Maskari,

Fatma Al Rashdi,

Laurent Poirel

Publication year - 2011

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.00481-11

Subject(s) - klebsiella pneumoniae , microbiology and biotechnology , carbapenem , transposition (logic) , plasmid , insertion sequence , biology , klebsiella , gene , sequence (biology) , escherichia coli , antibiotics , transposable element , genetics , genome , linguistics , philosophy

Klebsiella pneumoniae KP3 was isolated from a patient transferred from India to the Sultanate of Oman.K. pneumoniae KP3 was resistant to all β-lactams, including carbapenems, and expressed the carbapenem-hydrolyzing β-lactamase OXA-181, which differs from OXA-48 by four amino acid substitutions. Compared to OXA-48, OXA-181 possessed a very similar hydrolytic profile. Thebla OXA-181 gene was located on a 7.6-kb ColE-type plasmid and was linked to the insertion sequence ISEcp1 . The ISEcp1 -mediated one-ended transposition ofbla OXA-181 was also demonstrated.

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