Back to Search
Start Over
Proteomic insights into Helicobacter pylori coccoid forms under oxidative stress
- Source :
- Current microbiology. 57(4)
- Publication Year :
- 2008
-
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.
- Subjects :
- Proteomics
Proteome
Reductase
medicine.disease_cause
Applied Microbiology and Biotechnology
Microbiology
Superoxide dismutase
Bacterial Proteins
Microscopy, Electron, Transmission
medicine
Humans
Electrophoresis, Gel, Two-Dimensional
Heat shock
Gel electrophoresis
biology
Helicobacter pylori
Reverse Transcriptase Polymerase Chain Reaction
General Medicine
Gene Expression Regulation, Bacterial
biology.organism_classification
Molecular biology
Oxidative Stress
Biochemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
biology.protein
Oxidative stress
Heat-Shock Response
Subjects
Details
- ISSN :
- 03438651
- Volume :
- 57
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Current microbiology
- Accession number :
- edsair.doi.dedup.....364da7604b956099092c9f2502e1679a