Evolution of plasmid-coded resistance to broad-spectrum cephalosporins | Zendy

Christine Kliebe | Zendy; Berthold Nies | Zendy; Joachim Meyer | Zendy; Regina Tolxdorff-Neutzling | Zendy; B. Wiedemann | Zendy

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Evolution of plasmid-coded resistance to broad-spectrum cephalosporins

Author(s) -

Christine Kliebe,

Berthold Nies,

Joachim Meyer,

Regina Tolxdorff-Neutzling,

B. Wiedemann

Publication year - 1985

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.28.2.302

Subject(s) - cephalosporin , plasmid , mutant , biology , microbiology and biotechnology , beta lactamase , broad spectrum , point mutation , heteroduplex , klebsiella , gene , genetics , chemistry , escherichia coli , antibiotics , combinatorial chemistry

A clinical isolate of Klebsiella ozaenae with transferable resistance to broad-spectrum cephalosporins produces a beta-lactamase determined by plasmid pBP60. The beta-lactamase had the same isoelectric point as SHV-1 (7.6). From heteroduplex analysis, an extensive homology between the two bla genes could be deduced; therefore, the new beta-lactamase was designated SHV-2. Enzymatic studies revealed that SHV-2 was able to hydrolyze broad-spectrum cephalosporins due to an increased affinity of these compounds for the enzyme. The assumption that SHV-2 is a natural mutant of SHV-1 was strongly supported by the isolation of a laboratory mutant of SHV-1 that showed activities similar to those of SHV-2.

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