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Gene Review

sodC  -  superoxide dismutase

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

 
 
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Disease relevance of sodC

  • Sequence analysis of regions flanking the Salmonella typhimurium sodC gene encoding Cu,Zn-SOD demonstrates significant homology to lambda phage proteins, reflecting possible bacteriophage-mediated horizontal gene transfer of this determinant among pathogenic bacteria [1].
  • Overall the results of this work suggest that the duplicate sodC genes of Salmonella have evolved to respond to different sets of conditions encountered by bacteria inside the host and in the environment [2].
  • The predicted protein sequence shows only 58% identity to Escherichia coil SodC, and from this its chromosomal location and its immediate proximity to a phage gene, sodC, in Salmonella is speculated to have been acquired by bacteriophage-mediated horizontal transfer from an unknown donor [3].
  • The contribution of the Gifsy-1 prophage to virulence - undetectable in the presence of Gifsy-2 as prophage - becomes significant in cells that lack Gifsy-2 but carry the sodC gene integrated in the chromosome [4].
  • An analysis of the sodC genes present in available databases indicates that the same signal for lipid modification is also present in the sodC gene products from other mycobacteria and Gram-positive bacteria and, uniquely, in two distinct sodC gene products from the Gram-negative bacterium Salmonella typhimurium [5].
 

High impact information on sodC

  • Phage Gifsy-2 carries the sodC gene for a periplasmic [Cu,Zn]-superoxide dismutase previously implicated in the bacterial defences against killing by macrophages [4].
  • S. typhimurium, S. choleraesuis and S. dublin sodC mutants showed reduced lethality in a mouse model of oral infection and persisted in significantly lower numbers in livers and spleens after intraperitoneal infection, suggesting that [Cu,Zn]-SOD plays a role in pathogenicity, protecting Salmonella against oxygen radical-mediated host defences [3].
  • Evidence is also provided for an up-regulation of M. tuberculosis sodC in response to phagocytosis by human macrophages, suggesting that Cu,ZnSOD is involved in the mechanisms that facilitate mycobacterial intracellular growth [5].

References

  1. Periplasmic superoxide dismutase protects Salmonella from products of phagocyte NADPH-oxidase and nitric oxide synthase. De Groote, M.A., Ochsner, U.A., Shiloh, M.U., Nathan, C., McCord, J.M., Dinauer, M.C., Libby, S.J., Vazquez-Torres, A., Xu, Y., Fang, F.C. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  2. Differential accumulation of Salmonella[Cu, Zn] superoxide dismutases SodCI and SodCII in intracellular bacteria: correlation with their relative contribution to pathogenicity. Uzzau, S., Bossi, L., Figueroa-Bossi, N. Mol. Microbiol. (2002) [Pubmed]
  3. Bacterial copper- and zinc-cofactored superoxide dismutase contributes to the pathogenesis of systemic salmonellosis. Farrant, J.L., Sansone, A., Canvin, J.R., Pallen, M.J., Langford, P.R., Wallis, T.S., Dougan, G., Kroll, J.S. Mol. Microbiol. (1997) [Pubmed]
  4. Inducible prophages contribute to Salmonella virulence in mice. Figueroa-Bossi, N., Bossi, L. Mol. Microbiol. (1999) [Pubmed]
  5. Lipid modification of the Cu,Zn superoxide dismutase from Mycobacterium tuberculosis. D'orazio, M., Folcarelli, S., Mariani, F., Colizzi, V., Rotilio, G., Battistoni, A. Biochem. J. (2001) [Pubmed]
 
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