Publication: Inactivation of ahpC renders Stenotrophomonas maltophilia resistant to the disinfectant hydrogen peroxide
Issued Date
2019-05-15
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ISSN
15729699
00036072
00036072
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2-s2.0-85057135854
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Mahidol University
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SCOPUS
Bibliographic Citation
Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology. Vol.112, No.5 (2019), 809-814
Suggested Citation
Nisanart Charoenlap, Luksika Jiramonai, Jurairat Chittrakanwong, Naruemon Tunsakul, Skorn Mongkolsuk, Paiboon Vattanaviboon Inactivation of ahpC renders Stenotrophomonas maltophilia resistant to the disinfectant hydrogen peroxide. Antonie van Leeuwenhoek, International Journal of General and Molecular Microbiology. Vol.112, No.5 (2019), 809-814. doi:10.1007/s10482-018-1203-9 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/50178
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Title
Inactivation of ahpC renders Stenotrophomonas maltophilia resistant to the disinfectant hydrogen peroxide
Abstract
© 2018, Springer Nature Switzerland AG. Inactivation of ahpC, encoding alkyl hydroperoxide reductase, rendered Stenotrophomonas maltophilia more resistant to H 2 O 2 ; the phenotype was directly correlated with enhanced total catalase activity, resulting from an increased level of KatA catalase. Plasmid-borne expression of ahpC from pAhpC sm could complement all of the mutant phenotypes. Mutagenesis of the proposed AhpC peroxidactic and resolving cysteine residues to alanine (C47A and C166A) on the pAhpC sm plasmid diminished its ability to complement the ahpC mutant phenotypes, suggesting that the mutagenized ahpC was non-functional. As mutations commonly occur in bacteria living in hostile environment, our data suggest that point mutations in ahpC at codons required for the enzyme function (such as C47 and C166), the AhpC will be non-functional, leading to high resistance to the disinfectant H 2 O 2 .