ArticleAnnals of clinical microbiology and antimicrobials2015
Purification and characterization of a new β-lactamase OXA-205 from Pseudomonas aeruginosa.
Article in Annals of clinical microbiology and antimicrobials, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers, 1 of them a synthesis that pooled it.
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Who cites it
5 citing papers in PubMed, 1 synthesis or guideline pooled it, 23 citations in OpenAlex.
- Prioritization of Critical Factors for Surveillance of the Dissemination of Antibiotic Resistance inInternational journal of molecular sciences · 2023Pooled it
- Antarctic soil microbiomes encode structurally conserved and phylogenetically diverse beta-lactamases.iMetaOmics · 2026Article
- Bacterial diversity and resistome analysis of drinking water stored in cisterns from two First Nations communities in Manitoba, Canada.Microbiology spectrum · 2024Article
- Novel Antibiotic Resistance Genes Identified by Functional Gene Library Screening inInternational journal of molecular sciences · 2023Article
- Expression and purification of soluble recombinant β-lactamases using Escherichia coli as expression host and pET-28a as cloning vector.Microbial cell factories · 2022Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundWe have identified a novel class 1 integron (1503 bp), named In671 in a clinical Pseudomonas aeruginosa isolate. Integron sequence analysis revealed two gene cassettes, one coding for a new OXA-type β-lactamase designated as OXA-205 and the other coding for the aadB gene that is responsible for aminoglycoside resistance. The 266 amino acid sequence of OXA-205 revealed that this β-lactamase belongs to the Ambler class D showing highest sequence homology to the OXA-2 sub-lineage. Our objective was to purify and characterize β-lactamase OXA-205.
methodsEscherichia coli cells were transformed with a plasmid containing cloned bla OXA-205 gene from P. aeruginosa. Purification of overproduced OXA-205 consisted of a single ion-exchange chromatography step. SDS-PAGE and isoelectric focusing were performed to determine the molecular mass and pI, respectively. Size-exclusion chromatography was undertaken to determine the OXA-205 oligomerization state. Substrate hydrolysis reactions were employed to assess enzyme kinetic parameters.
resultsPurification of OXA-205 yielded the enzyme with >95 % purity (as verified by SDS-PAGE). Approximate yield of the protein was estimated to be 20 mg per liter of culture. OXA-205 had a pI at 8.1, molecular mass of 26 kDa and a monomeric native structure. Kinetic analysis revealed that OXA-205 hydrolyzed narrow spectrum substrates, including ampicillin, carbenicillin, oxacillin, penicillin G, cefazolin and cefuroxime. Additionally, we observed a substrate inhibition profile towards carbenicillin and oxacillin, but not with ampicillin or penicillin G. Our results also show that OXA-205 conferred unusually high (among class D β-lactamases) resistance towards inhibition by NaCl.
conclusionsOXA-205 can be considered a narrow spectrum monomeric β-lactamase that demonstrates unusually high resistance profile towards inhibition by NaCl.
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