Inactivation of ahpC renders Stenotrophomonas maltophilia resistant to the disinfectant hydrogen peroxide

  • Nisanart Charoenlap
  • Luksika Jiramonai
  • Jurairat Chittrakanwong
  • Naruemon Tunsakul
  • Skorn Mongkolsuk
  • Paiboon Vattanaviboon
Short Communication


Inactivation of ahpC, encoding alkyl hydroperoxide reductase, rendered Stenotrophomonas maltophilia more resistant to H2O2; the phenotype was directly correlated with enhanced total catalase activity, resulting from an increased level of KatA catalase. Plasmid-borne expression of ahpC from pAhpCsm could complement all of the mutant phenotypes. Mutagenesis of the proposed AhpC peroxidactic and resolving cysteine residues to alanine (C47A and C166A) on the pAhpCsm 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 H2O2.


AhpC Catalase Disinfectant H2O2 Stenotrohomonas maltophilia 



This study was funded by a Research Career Development Grant (RSA6080063) from the Thailand Research Fund to NC.

Authors’ contributions

NC and PV made a contribution to designing the study. NC, LJ, JC and NT were responsible for completing the experiments and data analysis. NC, SM and PV made a contribution to writing the manuscript. All authors read and approved the final manuscript.

Conflict of interest

The authors declare that they have no conflict of interest.


  1. Alexeyev MF (1999) The pKNOCK series of broad-host-range mobilizable suicide vectors for gene knockout and targeted DNA insertion into the chromosome of gram-negative bacteria. Biotechniques 26(5):824–826, 828CrossRefGoogle Scholar
  2. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. CrossRefPubMedGoogle Scholar
  3. Charoenlap N, Eiamphungporn W, Chauvatcharin N et al (2005) OxyR mediated compensatory expression between ahpC and katA and the significance of ahpC in protection from hydrogen peroxide in Xanthomonas campestris. FEMS Microbiol Lett 249(1):73–78. CrossRefPubMedGoogle Scholar
  4. Chauvatcharin N, Atichartpongkul S, Utamapongchai S et al (2005) Genetic and physiological analysis of the major OxyR-regulated katA from Xanthomonas campestris pv. phaseoli. Microbiology 151(Pt 2):597–605. CrossRefPubMedGoogle Scholar
  5. Chung CH, Fen SY, Yu SC et al (2015) Influence of oxyR on growth, biofilm formation, and mobility of Vibrio parahaemolyticus. Appl Environ Microbiol 82(3):788–796. CrossRefPubMedGoogle Scholar
  6. Crossman LC, Gould VC, Dow JM et al (2008) The complete genome, comparative and functional analysis of Stenotrophomonas maltophilia reveals an organism heavily shielded by drug resistance determinants. Genome Biol 9(4):R74. CrossRefPubMedPubMedCentralGoogle Scholar
  7. Dubbs JM, Mongkolsuk S (2007) Peroxiredoxins in bacterial antioxidant defense. Subcell Biochem 44:143–193CrossRefGoogle Scholar
  8. Guyot A, Turton JF, Garner D (2013) Outbreak of Stenotrophomonas maltophilia on an intensive care unit. J Hosp Infect 85(4):303–307. CrossRefPubMedGoogle Scholar
  9. Ieva R, Roncarati D, Metruccio MM et al (2008) OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms. Mol Microbiol 70(5):1152–1165. CrossRefPubMedGoogle Scholar
  10. Kovach ME, Elzer PH, Hill DS et al (1995) Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166(1):175–176. CrossRefPubMedGoogle Scholar
  11. Linley E, Denyer SP, McDonnell G et al (2012) Use of hydrogen peroxide as a biocide: new consideration of its mechanisms of biocidal action. J Antimicrob Chemother 67(7):1589–1596. CrossRefPubMedGoogle Scholar
  12. Ochoa-Sanchez LE, Vinuesa P (2017) Evolutionary genetic analysis uncovers multiple species with distinct habitat preferences and antibiotic resistance phenotypes in the Stenotrophomonas maltophilia complex. Front Microbiol 8:1548. CrossRefPubMedPubMedCentralGoogle Scholar
  13. Pan A, Balakrishna AM, Nartey W et al (2018) Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C. Free Radic Biol Med 115:252–265. CrossRefPubMedGoogle Scholar
  14. Romsang A, Leesukon P, Duangnkern J et al (2015) Mutation of the gene encoding monothiol glutaredoxin (GrxD) in Pseudomonas aeruginosa increases its susceptibility to polymyxins. Int J Antimicrob Agents 45(3):314–318. CrossRefPubMedGoogle Scholar
  15. Sambrook J, Russell DW (2001) Molecular cloning: a laboratory manual, 3rd edn. Cold Spring Harbor Laboratory, Cold Spring Harbor, NYGoogle Scholar
  16. Seaver LC, Imlay JA (2001) Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J Bacteriol 183(24):7173–7181. CrossRefPubMedPubMedCentralGoogle Scholar
  17. Srijaruskul K, Charoenlap N, Namchaiw P et al (2015) Regulation by SoxR of mfsA, which encodes a major facilitator protein Involved in paraquat resistance in Stenotrophomonas maltophilia. PLoS ONE 10(4):e0123699. CrossRefPubMedPubMedCentralGoogle Scholar
  18. Vattanaviboon P, Mongkolsuk S (2000) Expression analysis and characterization of the mutant of a growth-phase- and starvation-regulated monofunctional catalase gene from Xanthomonas campestris pv. phaseoli. Gene 241(2):259–265. CrossRefPubMedGoogle Scholar

Copyright information

© Springer Nature Switzerland AG 2018

Authors and Affiliations

  1. 1.Laboratory of BiotechnologyChulabhorn Research InstituteBangkokThailand
  2. 2.Program in Applied Biological Sciences: Environmental Health, Chulabhorn Graduate InstituteChulabhorn Royal AcademyBangkokThailand
  3. 3.Center of Excellence on Environmental Health and Toxicology, EHTMinistry of EducationBangkokThailand
  4. 4.Department of Biotechnology, Faculty of ScienceMahidol UniversityBangkokThailand
  5. 5.Center of Emerging Bacterial Infection, Faculty of ScienceMahidol UniversityBangkokThailand

Personalised recommendations