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

Hyojeong Yi; Jongwook Park; Kwang Hwi Cho; Heenam Stanley Kim

doi:10.1128/AAC.02252-19

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

Hyojeong Yi, Jongwook Park, Kwang Hwi Cho, Heenam Stanley Kim

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Highly conserved PenI-type class A β-lactamase in pathogenic members of Burkholderia 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 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.

Original language	English
Article number	e02252-19
Journal	Antimicrobial Agents and Chemotherapy
Volume	64
Issue number	6
DOIs	https://doi.org/10.1128/AAC.02252-19
Publication status	Published - 2020 Jun

Bibliographical note

Funding Information:
This work was supported by grants NRF-2018R1A2B2006456, 2018M3A9F3055923, and 2015M3C9A4053393 from the National Research Foundation (NRF) of the Republic of Korea. Additional support was provided by grant 2016R1A6A3A11935950 for research fellows from the NRF of the Republic of Korea to H.Y.

Publisher Copyright:
Copyright © 2020 American Society for Microbiology. All Rights Reserved.

Keywords

Antibiotic tolerance
ArgS
Arginine-tRNA synthetase
Stringent response

ASJC Scopus subject areas

Pharmacology
Pharmacology (medical)
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1128/AAC.02252-19

Cite this

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

abstract = "Highly conserved PenI-type class A β-lactamase in pathogenic members of Burkholderia 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 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.",

keywords = "Antibiotic tolerance, ArgS, Arginine-tRNA synthetase, Stringent response",

author = "Hyojeong Yi and Jongwook Park and Cho, {Kwang Hwi} and Kim, {Heenam Stanley}",

note = "Funding Information: This work was supported by grants NRF-2018R1A2B2006456, 2018M3A9F3055923, and 2015M3C9A4053393 from the National Research Foundation (NRF) of the Republic of Korea. Additional support was provided by grant 2016R1A6A3A11935950 for research fellows from the NRF of the Republic of Korea to H.Y. Publisher Copyright: Copyright {\textcopyright} 2020 American Society for Microbiology. All Rights Reserved.",

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doi = "10.1128/AAC.02252-19",

language = "English",

volume = "64",

journal = "Antimicrobial Agents and Chemotherapy",

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AU - Yi, Hyojeong

AU - Park, Jongwook

AU - Cho, Kwang Hwi

AU - Kim, Heenam Stanley

N1 - Funding Information: This work was supported by grants NRF-2018R1A2B2006456, 2018M3A9F3055923, and 2015M3C9A4053393 from the National Research Foundation (NRF) of the Republic of Korea. Additional support was provided by grant 2016R1A6A3A11935950 for research fellows from the NRF of the Republic of Korea to H.Y. Publisher Copyright: Copyright © 2020 American Society for Microbiology. All Rights Reserved.

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N2 - Highly conserved PenI-type class A β-lactamase in pathogenic members of Burkholderia 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 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.

AB - Highly conserved PenI-type class A β-lactamase in pathogenic members of Burkholderia 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 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.

KW - Antibiotic tolerance

KW - ArgS

KW - Arginine-tRNA synthetase

KW - Stringent response

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VL - 64

JO - Antimicrobial Agents and Chemotherapy

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ER -

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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

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