Table of Contents
Metal-Based Drugs
Volume 2008 (2008), Article ID 289490, 6 pages
http://dx.doi.org/10.1155/2008/289490
Research Article

Identification of Proteins Related to Nickel Homeostasis in Helicobater pylori by Immobilized Metal Affinity Chromatography and Two-Dimensional Gel Electrophoresis

1Institute of Life and Health Engineering, Jinan University, Guangzhou 510632, China
2Department of Chemistry and Open Laboratory of Chemical Biology, The University of Hong Kong, Hong Kong
3Department of Anatomy, The University of Hong Kong, Hong Kong

Received 28 June 2007; Accepted 21 October 2007

Academic Editor: Edward N. Baker

Copyright © 2008 Xuesong Sun et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

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.