Abstract
Helicobacter pylori, an etiological agent of gastroduodenal diseases, undergoes drastic morphological transition from spiral shape to coccoid form under oxidative stress. However, the knowledge of the specific expression profile in response to oxidative stress is relatively limited. Here, we report global proteomic analysis of H. pylori coccoids under oxidative stress. Two-dimensional gel electrophoresis analysis of H. pylori featuring coccoid revealed that 10 unique protein spots exhibit different expression profiles with comparison of that under normal microaerophilic condition. In total, seven proteins including superoxide dismutase, alkyl hydroperoxide reductase, urease G, and so forth were confirmed using matrix-assisted laser desorption/ionization time-of-flight/mass spectroscopy and then validated by reverse transcription–polymerase chain reaction, indicating that they play key roles in the physiological adaptation mechanisms of H. pylori to oxygen challenge. These data provide preliminary insights into H. pylori on coccoid generation under oxidative stress.
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Acknowledgments
We thank Dr. Youjun Feng, a visiting scholar in Faculty of Medical Laboratory Science, Third Military Medical University (present address: Department of Microbiology, University of Illinois at Urbana-Champaign (UIUC), USA) for critical reading of the manuscript. We are grateful to Dr. Zhi Rong Mou (Institute of Immunology, Third Military Medical University, China) for technical assistance in the utilization of ImageMasterTM 2D Elite version 3.10 software and MALDI-TOF-based peptide determination. This work was supported by the Chinese National Program for High Technology Research and Development (2003AA215020).
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Zeng, H., Guo, G., Mao, X.H. et al. Proteomic Insights into Helicobacter pylori Coccoid Forms Under Oxidative Stress. Curr Microbiol 57, 281–286 (2008). https://doi.org/10.1007/s00284-008-9190-0
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DOI: https://doi.org/10.1007/s00284-008-9190-0