Affiliation:
1. Department of Microbiology and Immunology, University of Texas Health Science Center San Antonio, San Antonio, Texas 78284,1 and
2. Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48109-06202
Abstract
ABSTRACT
In contrast to the apparent paucity of
Mycobacterium tuberculosis
response to reactive oxygen intermediates, this organism has evolved a specific response to nitric oxide challenge. Exposure of
M. tuberculosis
to NO donors induces the synthesis of a set of polypeptides that have been collectively termed Nox. In this work, the most prominent Nox polypeptide, Nox16, was identified by immunoblotting and by N-terminal sequencing as the α-crystallin-related, 16-kDa small heat shock protein, sHsp16. A panel of chemically diverse donors of nitric oxide, with the exception of nitroprusside, induced sHsp16 (Nox16). Nitroprusside, a coordination complex of Fe
2+
with a nitrosonium (NO
+
) ion, induced a 19-kDa polypeptide (Nox19) homologous to the nonheme bacterial ferritins. We conclude that the NO response in
M. tuberculosis
is dominated by increased synthesis of the α-crystallin homolog sHsp16, previously implicated in stationary-phase processes and found in this study to be a major
M. tuberculosis
protein induced upon exposure to reactive nitrogen intermediates.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
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