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Mutations in ArgS Arginine-tRNA Synthetase Confer Additional Antibiotic Tolerance Protection to Extended-Spectrum-?-Lactamase-Producing Burkholderia thailandensis.

ABSTRACT: Highly conserved PenI-type class A ?-lactamase in pathogenic members of Burkholderia species can evolve to extended-spectrum ?-lactamase (ESBL), which exhibits hydrolytic activity toward third-generation cephalosporins, while losing its activity toward the original penicillin substrates. We describe three single-amino-acid-substitution mutations in the ArgS arginine-tRNA synthetase that confer extra antibiotic tolerance protection to ESBL-producing Burkholderia thailandensis This pathway can be exploited to evade antibiotic tolerance induction in developing therapeutic measures against Burkholderia species, targeting their essential aminoacyl-tRNA synthetases.

SUBMITTER: Yi H

PROVIDER: S-EPMC7269490 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Mutations in ArgS Arginine-tRNA Synthetase Confer Additional Antibiotic Tolerance Protection to Extended-Spectrum-β-Lactamase-Producing Burkholderia thailandensis.

Yi Hyojeong H Park Jongwook J Cho Kwang-Hwi KH Kim Heenam Stanley HS

Antimicrobial agents and chemotherapy 20200521 6

Highly conserved PenI-type class A β-lactamase in pathogenic members of <i>Burkholderia</i> species can evolve to extended-spectrum β-lactamase (ESBL), which exhibits hydrolytic activity toward third-generation cephalosporins, while losing its activity toward the original penicillin substrates. We describe three single-amino-acid-substitution mutations in the ArgS arginine-tRNA synthetase that confer extra antibiotic tolerance protection to ESBL-producing <i>Burkholderia thailandensis</i> This p ...[more]

PMID: 32205346

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