Sun Xuesong, Ge Ruiguang, Chiu Jen-Fu, Sun Hongzhe, He Qing-Yu
Institute of Life and Health Engineering, Jinan University, Guangzhou 510632, China.
Met Based Drugs. 2008;2008:289490. doi: 10.1155/2008/289490.
Helicobacter pylori (H. pylori) is a widespread human pathogen causing peptic ulcers and chronic gastritis. Maintaining nickel homeostasis is crucial for the establishment of H. pylori infection in humans. We used immobilized-nickel affinity chromatography to isolate Ni-related proteins from H. pylori cell extracts. Two-dimensional gel electrophoresis and mass spectrometry were employed to separate and identify twenty two Ni-interacting proteins in H. pylori. These Ni-interacting proteins can be classified into several general functional categories, including cellular processes (HspA, HspB, TsaA, and NapA), enzymes (Urease, Fumarase, GuaB, Cad, PPase, and DmpI), membrane-associated proteins (OM jhp1427 and HpaA), iron storage protein (Pfr), and hypothetical proteins (HP0271, HP jhp0216, HP jhp0301, HP0721, HP0614, and HP jhp0118). The implication of these proteins in nickel homeostasis is discussed.
幽门螺杆菌（H. pylori）是一种广泛存在的人类病原体，可导致消化性溃疡和慢性胃炎。维持镍稳态对于幽门螺杆菌在人体内建立感染至关重要。我们使用固定化镍亲和色谱法从幽门螺杆菌细胞提取物中分离与镍相关的蛋白质。采用二维凝胶电泳和质谱法分离并鉴定了幽门螺杆菌中22种与镍相互作用的蛋白质。这些与镍相互作用的蛋白质可分为几个一般功能类别，包括细胞过程（HspA、HspB、TsaA和NapA）、酶（脲酶、延胡索酸酶、GuaB、Cad、焦磷酸酶和DmpI）、膜相关蛋白（外膜蛋白jhp1427和HpaA）、铁储存蛋白（Pfr）以及假想蛋白（HP0271、HP jhp0216、HP jhp0301、HP0721、HP0614和HP jhp0118）。本文讨论了这些蛋白质在镍稳态中的作用。
