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J. Bacteriol., 07 1996, 4301-4305, Vol 178, No. 14
TD Moore and PF Sparling
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.
Copyright © 1996, American Society for Microbiology
Interruption of the gpxA gene increases the sensitivity of Neisseria meningitidis to paraquat
Department of Medicine, University of North Carolina at Chapel Hill, 27599-7030, USA.
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