About this Biochemistry, Genetics and Molecular Biology article

Proteomic analysis of proteins expressed by Helicobacter pylori under oxidative stress by Ming-Hong Chuang; Ming-Shiang Wu; Jou-Town Lin; Shyh-Horng Chiou is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

## Abstract __Helicobacter pylori__ is a spiral, slow growing gram‐negative microaerophilic bacterium. It has been shown to be the etiological agent of gastroduodenal diseases, such as chronic gastritis, gastric and duodenal ulcers, and gastric cancer. To address the influence of oxidative stress and its underlying mechanisms, we have compared proliferation, urease activity and protein expression profile of __H. pylori__ incubated under normal microaerophilic (5% O~2~) and aerobic stress (20% O~2~) conditions. Oxidative‐stress cells displayed coccoid morphology and time‐dependent decrease in proliferation. The urease activity was completely abrogated after 32 h. We have further compared the protein expression profiles of __H. pylori__ under normal growing and oxidative‐stress conditions by a global proteomic analysis, which includes high‐resolution 2‐DE followed by MALDI‐TOF‐MS and bioinformatic databases search/peptide‐mass comparison. The results revealed that more than ten proteins were differentially expressed under oxidative stress. Most notably, the protein expression levels of urease accessory protein E (UreE, an essential metallochaperone for urease activity) and alkylhydro

Author

Ming-Hong Chuang; Ming-Shiang Wu; Jou-Town Lin; Shyh-Horng Chiou

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley; Research Square (ISSN 1615-9853)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)