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J. Biol. Chem., Vol. 275, Issue 43, 33883-33889, October 27, 2000
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From the Leishmania sp. protozoa are
introduced into a mammalian skin by a sandfly vector, whereupon they
encounter increased temperature and toxic oxidants generated during
phagocytosis. We studied the effects of 37 °C "heat shock" or
sublethal menadione, which generates superoxide and hydrogen peroxide,
on Leishmania chagasi virulence. Both heat and menadione
caused parasites to become more resistant to
H2O2-mediated toxicity. Peroxide resistance was
also induced as promastigotes developed in culture from logarithmic to
their virulent stationary phase form. Peroxide resistance was not
associated with an increase in reduced thiols (trypanothione and
glutathione) or increased activity of ornithine decarboxylase, which is
rate-limiting in trypanothione synthesis. Membrane lipophosphoglycan
increased in size as parasites developed to stationary phase but not
after environmental exposures. Instead, parasites underwent a heat
shock response upon exposure to heat or sublethal menadione, detected by increased levels of HSP70. Transfection of promastigotes with L. chagasi HSP70 caused a heat-inducible increase in
resistance to peroxide, implying it is involved in antioxidant defense.
We conclude that leishmania have redundant mechanisms for resisting toxic oxidants. Some are induced during developmental change and others
are induced in response to environmental stress.
Inducible Resistance to Oxidant Stress in the Protozoan
Leishmania chagasi*
§,§,
,,§, and§¶¶¶
Veterans Affairs Medical Center, the
§ Departments of Internal Medicine and Microbiology, and the
¶ Interdisciplinary Immunology Program, University of Iowa,
Iowa City, Iowa 52242 and §§ Haskins
Laboratories and the Departments of Biology and Chemistry, Pace
University, New York, New York 10038
*
This work was supported by Veterans Affairs Merit Review
grants (to M. E. W., B. E. B., and B. E. B.) and National
Institutes of Health Grants AI32135, DK/AI52550 (to M. E. W.),
AI34954 (to B. E. B.), and HL45135 (to B. E. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Current address: Dept. of Biochemistry and Biophysics, Texas
A&M University, College Station, TX 77843-2128.
**
Current address: Tulane School of Medicine, New Orleans, LA 70112.
Current address: Family Medical Center, Davenport, IA 52806.
¶¶
To whom correspondence should be addressed. Tel.:
319-356-3169; Fax: 319-384-7208; E-mail: mary-wilson@uiowa.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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