Functional significance of a periplasmic Mn-superoxide dismutase from Aeromonas hydrophila

J Appl Microbiol. 2004;96(4):828-33. doi: 10.1111/j.1365-2672.2004.02231.x.

Abstract

Aims: A better understanding of the role of superoxide dismutases (SODs) from Aeromonas hydrophila and particularly the Mn-SOD which shares a peculiar localization within the bacterial periplasm and is only detected during the stationary phase of growth.

Methods and results: A. hydrophila ATCC 7966 can express two distinct SODs: an Fe-SOD and an Mn-SOD. Using insertional mutagenesis, an Mn-SOD-deficient mutant was isolated. After growth of this mutant under conditions leading to the expression of an Mn-SOD, only the Fe-SOD could be detected in nondenaturing PAGE. Study of its response to the oxidative stress showed that the Mn-SOD was not implicated in the protection against intracellular superoxide but defended the bacterial cells against environmental superoxide.

Conclusions: By protecting the bacteria against external superoxide, the role of the Mn-SOD from A. hydrophila is equivalent to that of the Cu/Zn-SOD from the well-studied Escherichia coli.

Significance and impact of the study: The function of this Mn-SOD is in agreement with its periplasmic localization and may confer an advantage on the bacteria such as a virulence factor in cases of pathogenicity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aeromonas hydrophila / enzymology*
  • Mutagenesis, Insertional
  • Oxidative Stress
  • Superoxide Dismutase / genetics
  • Superoxide Dismutase / physiology*

Substances

  • Superoxide Dismutase