Abstract
Antioxidant enzymes are thought to be important for the survival of pathogenic Neisseria species. We have further characterized the glutathione peroxidase homolog gene (gpxA), which we recently isolated from Neisseria meningitidis FAM20 (T.D.E. Moore and P.F. Sparling, Infect. Immun. 63:1603-1607, 1995). GpxA was found to be produced constitutively in vivo. An isogenic, omega insertion mutant in the gpxA gene was constructed and characterized. The gpxA insertion mutant was much more sensitive to the oxidative stress caused by paraquat and slightly more sensitive to hydrogen peroxide. This is the first demonstration of a phenotype arising from a mutation of a glutathione peroxidase homolog gene in a prokaryotic organism. Protection of the cell by GpxA from the effects of oxidative stress caused by aerobic metabolism may contribute to the ability of Neisseria meningitidis to cause disease in the human host.