Functional significance of a periplasmic Mn-superoxide dismutase from Aeromonas hydrophila |
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Authors: | Leclère V Béchet M Blondeau R |
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Affiliation: | Laboratoire de Microbiologie, Batiment SN2, Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France. valerie.leclere@univ-lillel.fr |
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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. |
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Keywords: | Aeromonas hydrophila oxidative stress periplasm superoxide dismutase |
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