251. Overexpression of a hydrogen peroxide-resistant periplasmic Cu,Zn superoxide dismutase protects Escherichia coli from macrophage killing.
- Author
-
Battistoni A, Donnarumma G, Greco R, Valenti P, and Rotilio G
- Subjects
- Animals, Cattle, Cell Line, Drug Resistance, Enzyme Inhibitors pharmacology, Escherichia coli enzymology, Escherichia coli genetics, Humans, Macrophage Activation, Mice, Superoxide Dismutase antagonists & inhibitors, Escherichia coli physiology, Gene Expression, Hydrogen Peroxide pharmacology, Macrophages physiology, Superoxide Dismutase genetics, Superoxide Dismutase metabolism
- Abstract
We have studied the effect of H2O2 on the activity of the Escherichia coli Cu,ZnSOD showing that, unlike the bovine enzyme, this bacterial Cu,ZnSOD is highly resistant to inactivation by hydrogen peroxide. In view of the key role played by oxygen radicals in bacterial killing by phagocytes, we have tested the ability of E. coli strains expressing different amounts of Cu,ZnSOD in the periplasmic space to survive the phagocytic attack of activated macrophages. Overexpression of the enzyme effectively protected the bacterial cell from macrophage killing. The results obtained support the hypothesis that in pathogenic bacteria periplasmic Cu,ZnSOD may reduce the oxyradical damages induced by the respiratory burst and therefore be important in virulence.
- Published
- 1998
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