본문 바로가기
HOME> 논문 > 논문 검색상세

논문 상세정보

The journal of microbiology v.47 no.5, 2009년, pp.624 - 632   SCI SCIE 피인용횟수: 2
본 등재정보는 저널의 등재정보를 참고하여 보여주는 베타서비스로 정확한 논문의 등재여부는 등재기관에 확인하시기 바랍니다.

Identification of the Vibrio vulnificus ahpC1 Gene and Its Influence on Survival under Oxidative Stress and Virulence

Baek, Woon-Ki    (National Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Center for Agricultural Biomaterials, and Research Institute for Agriculture and Life Sciences, Seoul National University   ); Lee, Hyun-Sung    (National Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Center for Agricultural Biomaterials, and Research Institute for Agriculture and Life Sciences, Seoul National University   ); Oh, Man-Hwan    (National Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Center for Agricultural Biomaterials, and Research Institute for Agriculture and Life Sciences, Seoul National University   ); Koh, Myung-Jin    (National Research Laboratory of Molecular Microbiology and Toxicology, Department of Agricultural Biotechnology, Center for Agricultural Biomaterials, and Research Institute for Agriculture and Life Sciences, Seoul National University   ); Kim, Kun-Soo    (Department of Life Science and Interdisciplinary Pro  ); Choi, Sang-Ho  
  • 초록

    Pathogens have evolved sophisticated mechanisms to survive oxidative stresses imposed by host defense systems, and the mechanisms are closely linked to their virulence. In the present study, ahpC1, a homologue of Escherichia coli ahpC encoding a peroxiredoxin, was identified among the Vibrio vulnificus genes specifically induced by exposure to $H_2O_2$ . In order to analyze the role of AhpC1 in the pathogenesis of V. vulnificus, a mutant, in which the ahpC1 gene was disrupted, was constructed by allelic exchanges. The ahpC1 mutant was hypersusceptable to killing by reactive oxygen species (ROS) such as $H_2O_2$ and t-BOOH, which is one of the most commonly used hydroperoxides in vitro. The purified AhpC1 reduced $H_2O_2$ in the presence of AhpF and NADH as a hydrogen donor, indicating that V. vulnificus AhpC1 is a NADH-dependent peroxiredoxin and constitutes a peroxide reductase system with AhpF. Compared to wild type, the ahpC1 mutant exhibited less cytotoxicity toward INT-407 epithelial cells in vitro and reduced virulence in a mouse model. In addition, the ahpC1 mutant was significantly diminished in growth with INT-407 epithelial cells, reflecting that the ability of the mutant to grow, survive, and persist during infection is also impaired. Consequently, the combined results suggest that AhpC1 and the capability of resistance to oxidative stresses contribute to the virulence of V. vulnificus by assuring growth and survival during infection.


  • 주제어

    V.   vulnificus ahpC1 .   oxidative stress .   virulence.  

  • 참고문헌 (31)

    1. Brenot, A., K.Y. King, and M.G. Caparon. 2005. The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Mol. Microbiol. 55, 221-234 
    2. Goo, S.Y., H.J. Lee, W.H. Kim, K.L. Han, D.K. Park, H.J. Lee, S.M. Kim, K.S. Kim, K.H. Lee, and S.J. Park. 2006. Identification of OmpU of Vibrio vulnificus as a fibronectin-binding protein and its role in bacterial pathogenesis. Infect. Immun. 74, 5586-5594 
    3. Hase, C.C. and R.A. Finkelstein. 1993. Bacterial extracellular zinc containing metalloproteinases. Microbiol. Rev. 57, 823-837 
    4. Jones, M.K. and J.D. Oliver. 2009. Vibrio vulnificus: Disease and pathogenesis. Infect. Immun. (Epub ahead of print) 
    5. Park, N.Y., J.H. Lee, M.W. Kim, H.G. Jeong, B.C. Lee, T.S. Kim, and S.H. Choi. 2006. Identificatioin of Vibrio vulnificus wbpP gene and evaluation of its role in virulence. Infect. Immun. 74, 721-728 
    6. Storz, G. and M. Zheng. 2000. Oxidative stress, p. 47-59. In G. Storz and R. Hennge-Aronis (eds.), Bacterial stress responses. American Society for Microbiology, Washington, D.C., USA 
    7. Poole, L.B. 2005. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Arch. Biochem. Biophys. 433, 240-254 
    8. Shinoda, S., S. Miyoshi, H. Yamanaka, and N. Miyoshi-Nakahara. 1985. Some properties of Vibrio vulnificus hemolysin. Microbiol. Immunol. 29, 583-590 
    9. Zheng, M., X. Wang, B. Doan, K.A. Lewis, T.D. Schneider, and G. Storz. 2001. Computation-directed identification of OxyR DNA binding sites in Escherichia coli. J. Bacteriol. 183, 4571-4579 
    10. Christman, M.F., R.W. Morgan, F.S. Jacobson, and B.N. Ames. 1985. Positive control of a regulon for defences against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell. 41, 753-762 
    11. Master, S.S., B. Springer, P. Sander, E.C. Boettger, V. Deretic, and G.S. Timmins. 2002. Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC1 in resistance to peroxynitrite and stage-specific survival in macrophages. Microbiology 148, 3139-3144 
    12. Poole, L.B. 2003. Bacterial peroxiredoxins, p. 81-101. In H.J. Forman, J.M. Fukuto, and M. Torres (eds.), Signal transduction by reactive oxygen and nitrogen species: Pathways and chemical principles, Kluwer Academic, MA, USA 
    13. Jeong, H.G. and S.H. Choi. 2008. Evidence that AphB essential for the virulence of Vibrio vulnificus is a global regulator. J. Bacteriol. 190, 3768-3773 
    14. J$\"{o}$nsson, T.J., H.R. Ellis, and L.B. Poole. 2007. Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC1 of the bacterial alkyl hydroperoxide reductase system. Biochemistry 46, 5709-5721 
    15. Miller, R.A. and B.E. Britigan. 1997. Role of oxidants in microbial pathophysiology. Clin. Microbiol. Rev. 10, 1-18 
    16. Park, K.J., M.J. Kang, S.H. Kim, H.J. Lee, J.K. Lim, S.H. Choi, S.J. Park, and K.H. Lee. 2004. Isolation and characterization of rpoS in a pathogenic bacterium, Vibrio vulnificus: Role of $\sigma^S$ in survival of exponential phase cells under oxidative stress. J. Bacteriol. 186, 3304-3312 
    17. Strom, M. and R.N. Paranjpye. 2000. Epidemiology and pathogenesis of Vibrio vulnificus. Microbes Infect. 2, 177-188 
    18. Wang, G., A.A. Olczak, J.P. Walton, and R.J. Maier. 2005. Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonization. Infect. Immun. 73, 378-384 
    19. Jeong, W., M.K. Cha, and I.H. Kim. 2000. Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/alkyl hydroperoxide peroxidase C (AhpC) family. J. Biol. Chem. 275, 2924-2930 
    20. Lee, J.H., M.W. Kim, B.S. Kim, S.M. Kim, B.C. Lee, T.S. Kim, and S.H. Choi. 2007. Identification and characterization of the Vibrio vulnificus rtxA essential for cytotoxicity in vitro and virulence in mice. J. Microbiol. 45, 146-152     
    21. Kang, I.H., J.S. Kim, and J.K. Lee. 2007. The virulence of Vibrio vulnificus is affected by the cellular level of superoxide dismutase activity. J. Microbiol. Biotechnol. 17, 1399-1402     
    22. Linkous, D.A. and J.D. Oliver. 1999. Pathogenesis of Vibrio vulnificus. FEMS Microbiol. Lett. 174, 207-214 
    23. Wood, M.J., E.C. Andrade, and G. Storz. 2003. The redox domain of the Yap1p transcription factor contains two disulfide bonds. Biochemistry 42, 11982-11991 
    24. Falkow, S. 1988. Molecular Koch's postulates applied to microbial pathogenicity. Rev. Infect. Dis. 10, 274-276 
    25. Mekalanos, J.J. 1992. Environmental signals controlling expression of virulence determinants in bacteria. J. Bacteriol. 174, 1-7 
    26. Fang, F.C., M.A. DeGroote, J.W. Foster, A.J. B$\ddot{a}$umler, U. Ochsner, T. Testerman, S. Bearson, J.C. Gi$\acute{a}$rd, Y. Xu, G. Campbell, and T. Laessig. 1999. Virulent Salmonella typhimurium has two periplasmic Cu, Zn-superoxide dismutases. Proc. Natl. Acad. Sci. USA 13, 7502-7507 
    27. Reed, L.J. and H. Muench. 1938. A simple method of estimating fifty percent endpoints. Am. J. Hyg. 27, 439-497 
    28. Oka, A., H. Sugisaki, and M. Takanami. 1981. Nucleotide sequence of the kanamycin resistance transposon Tn903. J. Mol. Biol. 147, 217-226 
    29. Oh, M.H., S.M. Lee, D.H. Lee, and S.H. Choi. 2009. Regulation of the Vibrio vulnificus hupA gene by temperature alteration and cyclic AMP receptor protein and evaluation of its role in virulence. Infect. Immun. 77, 1208-1215 
    30. Miller, V.L. and J.J. Mekalanos. 1988. A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J. Bacteriol. 170, 2575-2583 
    31. Milton, D.L., R. O'Toole, P. Horstedt, and H. Wolf-Watz. 1996. Flagellin A is essential for the virulence of Vibrio anguillarum. J. Bacteriol. 178, 1310-1319 
  • 이 논문을 인용한 문헌 (2)

    1. 2010. "" The journal of microbiology, 48(1): 129~133     
    2. 2015. "" Journal of microbiology and biotechnology, 25(8): 1380~1389     

 활용도 분석

  • 상세보기

    amChart 영역
  • 원문보기

    amChart 영역

원문보기

무료다운로드
  • 원문이 없습니다.
유료다운로드

유료 다운로드의 경우 해당 사이트의 정책에 따라 신규 회원가입, 로그인, 유료 구매 등이 필요할 수 있습니다. 해당 사이트에서 발생하는 귀하의 모든 정보활동은 NDSL의 서비스 정책과 무관합니다.

원문복사신청을 하시면, 일부 해외 인쇄학술지의 경우 외국학술지지원센터(FRIC)에서
무료 원문복사 서비스를 제공합니다.

NDSL에서는 해당 원문을 복사서비스하고 있습니다. 위의 원문복사신청 또는 장바구니 담기를 통하여 원문복사서비스 이용이 가능합니다.

이 논문과 함께 출판된 논문 + 더보기