Infection and Immunity, July 2000, p. 3861-3866, Vol. 68, No. 7
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Copyright © 2000, American Society for Microbiology. All rights reserved.

andDepartment of Zoology and Genetics, Iowa State University, Ames, Iowa 50011
Received 10 December 1999/Returned for modification 17 February 2000/Accepted 30 March 2000
All aerobic organisms have mechanisms that protect against oxidative compounds. Catalase, peroxidase, superoxide dismutase, glutathione, and thioredoxin are widely distributed in many taxa and constitute elements of a nearly ubiquitous antioxidant metabolic strategy. Interestingly, the regulatory mechanisms that control these elements are rather different depending on the nature of the oxidative stress and the organism. Catalase is well documented to play an important role in protecting cells from oxidative stress. In particular, pathogenic bacteria seem to use this enzyme as a defensive tool against attack by the host. To investigate the significance of catalase in hostile environments, we made catalase deletion mutations in two different B. abortus strains and used two-dimensional gel analysis, survival tests, and adaptation experiments to explore the behavior and role of catalase under several oxidative stress conditions. These studies show that B. abortus strains that do not express catalase activity exhibit increased sensitivity to hydrogen peroxide. We also demonstrate that catalase expression is regulated in this species, and that preexposure to a sublethal concentration of hydrogen peroxide allows B. abortus to adapt so as to survive subsequent exposure to higher concentrations of hydrogen peroxide.
Present address: Department of Ophthalmology and Visual Science,
College of Medicine, The Catholic University of Korea, and Catholic
Research Institute of Medical Sciences, 505 Banpo-dong, Seocho-ku,
Seoul, Korea.
Present address: 3921 Omeara St., Houston, TX 77025.
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