CTX-M-5, a novel cefotaxime-hydrolyzing β-lactamase from an outbreak of Salmonella typhimurium in Latvia

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dc.contributor.authorBradford, Patricia A.
dc.contributor.authorYang, Youjun
dc.contributor.authorSahm, Daniel
dc.contributor.authorGrope, Ilze
dc.contributor.authorGardovska, Dace
dc.contributor.authorStorch, Gregory
dc.contributor.institutionDepartment of Paediatrics
dc.date.accessioned2021-08-31T08:35:08Z
dc.date.available2021-08-31T08:35:08Z
dc.date.issued1998-08
dc.description.abstractAt a children's hospital in Riga, Latvia, isolates identified as Salmonella typhimurium were found to be resistant to expanded-spectrum cephalosporins. Two of the resistant strains were analyzed for the mechanism of cephalosporin resistance. Isoelectric focusing revealed a common β- lactamase with a pI of 8.8. In addition, one of the strains produced a pI 7.6 β-lactamase. A transconjugant producing only the pI 7.6 enzyme was susceptible to expanded-spectrum cephalosporins; therefore, this enzyme was most likely SHV-1. Transformants producing only the pI 8.8 β-lactamase were resistant to cefotaxime and aztreonam but were susceptible or intermediate to ceftazidime. A substrate profile determined spectrophotometrically with purified enzyme revealed potent activity against cefotaxime, with a relative k(cat) value of 95 (benzylpenicillin equal to 100). The enzyme showed lower relative k(cat) values for ceftazidime (3.3) and aztreonam (9.3). In addition, the enzyme was inhibited by clavulanate, sulbactam and tazobactam, with 50% inhibitory concentrations of 19, 100, and 3.4 nM, respectively. These results indicated the presence of an unusual extended-spectrum β- lactamase. The gene expressing the pI 8.8 β-lactamase was cloned. Nucleotide sequencing revealed a β-lactamase gene that differs from the gene encoding CTX-M-2, which also originated from S. typhimurium, by 11 nucleotides, 4 of which result in amino acid substitutions: Ala27Thr, Val230Gly, Glu254Ala, and Ile278Val. These results indicated the presence of a novel extended-spectrum β-lactamase, designated CTX-M-5, that specifically confers resistance to cefotaxime.en
dc.description.statusPeer reviewed
dc.format.extent5
dc.format.extent165650
dc.identifier.citationBradford, P A, Yang, Y, Sahm, D, Grope, I, Gardovska, D & Storch, G 1998, 'CTX-M-5, a novel cefotaxime-hydrolyzing β-lactamase from an outbreak of Salmonella typhimurium in Latvia', Antimicrobial Agents and Chemotherapy, vol. 42, no. 8, pp. 1980-1984. https://doi.org/10.1128/aac.42.8.1980
dc.identifier.doi10.1128/aac.42.8.1980
dc.identifier.issn0066-4804
dc.identifier.urihttps://dspace.rsu.lv/jspui/handle/123456789/6132
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=0031926751&partnerID=8YFLogxK
dc.identifier.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC105719/
dc.language.isoeng
dc.relation.ispartofAntimicrobial Agents and Chemotherapy
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subject3.2 Clinical medicine
dc.subject3.1 Basic medicine
dc.subject1.1. Scientific article indexed in Web of Science and/or Scopus database
dc.subjectPharmacology
dc.subjectPharmacology (medical)
dc.subjectInfectious Diseases
dc.subjectSDG 3 - Good Health and Well-being
dc.titleCTX-M-5, a novel cefotaxime-hydrolyzing β-lactamase from an outbreak of Salmonella typhimurium in Latviaen
dc.type/dk/atira/pure/researchoutput/researchoutputtypes/contributiontojournal/article

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