Helicobacter pylori Thioredoxin Is an Arginase Chaperone and Guardian against Oxidative and Nitrosative Stresses

The gastric human pathogen Helicobacter pylori faces formidable challenges in the stomach including reactive oxygen and nitrogen intermediates. Here we demonstrate that arginase activity, which inhibits host nitric oxide production, is post-translationally stimulated by H. pylori thioredoxin (Trx) 1...

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Bibliographic Details
Published in:The Journal of biological chemistry 2006-02, Vol.281 (6), p.3290-3296
Main Authors: McGee, David J., Kumar, Sateesh, Viator, Ryan J., Bolland, Jeffrey R., Ruiz, Julio, Spadafora, Domenico, Testerman, Traci L., Kelly, David J., Pannell, Lewis K., Windle, Henry J.
Format: Article
Language:English
Subjects:
Arginase - chemistry
Chaperonin 60 - chemistry
Chromatography, Affinity
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Escherichia coli - metabolism
Helicobacter pylori
Helicobacter pylori - metabolism
Humans
Mass Spectrometry
Membrane Proteins - metabolism
Molecular Chaperones - metabolism
Mutation
Nitrogen - chemistry
Nitrogen - metabolism
Oxidation-Reduction
Oxidative Stress
Peptides - chemistry
Plasmids - metabolism
Reactive Oxygen Species
Spectrometry, Fluorescence
Stomach - microbiology
Thioredoxins - metabolism
Ultracentrifugation
Urease - chemistry
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Summary:The gastric human pathogen Helicobacter pylori faces formidable challenges in the stomach including reactive oxygen and nitrogen intermediates. Here we demonstrate that arginase activity, which inhibits host nitric oxide production, is post-translationally stimulated by H. pylori thioredoxin (Trx) 1 but not the homologous Trx2. Trx1 has chaperone activity that renatures urea- or heat-denatured arginase back to the catalytically active state. Most reactive oxygen and nitrogen intermediates inhibit arginase activity; this damage is reversed by Trx1, but not Trx2. Trx1 and arginase equip H. pylori with a “renox guardian” to overcome abundant nitrosative and oxidative stresses encountered during the persistence of the bacterium in the hostile gastric environment.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M506139200