Helicobacter pylori thioredoxin is an arginase chaperone and guardian against oxidative and nitrosative stresses
Helicobacter pylori thioredoxin is an arginase chaperone and guardian against oxidative and nitrosative stresses
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DOI：
10.1074/jbc.m506139200
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发表时间：
2006-02-10
影响因子：
4.8
通讯作者：
Windle, HJ
中科院分区：
文献类型：
--
作者：
McGee, DJ;Kumar, S;Windle, HJ
人类胃部病原体幽门螺杆菌在胃部面临着包括活性氧和氮中间体在内的巨大挑战。在这里，我们证明抑制宿主一氧化氮产生的精氨酸酶活性受到幽门螺杆菌硫氧还蛋白 (Trx) 1 的翻译后刺激，但不是同源的 Trx2。 Trx1 具有伴侣活性，可使尿素或热变性的精氨酸酶恢复到催化活性状态。大多数活性氧和氮中间体抑制精氨酸酶活性；这种损害可以被 Trx1 逆转，但不能被 Trx2 逆转。 Trx1 和精氨酸酶为幽门螺杆菌配备了“renox 守护者”，以克服细菌在恶劣的胃环境中持续存在时遇到的大量亚硝化和氧化应激。
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.