Related Experiment Videos
The rapid detection of low molecular mass proteins differentially expressed under biological stress for four
Sean O Hynes1, Jim McGuire, Tobias Falt
1Department of Medical Microbiology, Dermatology and Infection, Lund University, Sweden.
Abstract:
Helicobacter pylori is one of the most prevalent human pathogens in the world and is the aetiological agent of gastritis, peptic ulcer disease and gastric malignancies. In addition H. pylori and other novel members of the genus are capable of successfully colonising the bile-rich niche of the upper intestine and are associated with a diverse range of intestinal pathologies. Surface-enhanced laser desorption/ionisation-time of flight mass spectrometry was used to analyse surface extracts from H. pylori, Helicobacter bilis, Helicobacter pullorum and "Helicobacter sp. flexispira" to characterise cell surface changes following bile stress. The system detected two distinct response patterns to bile stress on the cell surface of Helicobacter spp. in vitro. The first involved the increase under bile stress of peaks at 7.6 and 7.9 kDa for H. billis and H. pullorum, respectively. In contrast both "Helicobacter sp. flexispira" and a clinical isolate of H. pylori had similar response profiles to bile stress. Both strains had at least three low mass peaks decreased under bile stress and a single peak induced by bile stress. The present study has established the use of ProteinChip(R) technology to analyse helicobacter-related proteomics. Specifically this study has established that different patterns are generated in response to bile stress among various pathogenic Helicobacter spp. which may give insights into the ability of these strains to colonise different niches.
Insights
This study reveals distinct Helicobacter pylori and related species surface protein changes under bile stress. These proteomic patterns may explain how these bacteria colonize different intestinal environments.
Area of Science:
- Microbiology
- Proteomics
- Gastroenterology
Background:
- Helicobacter pylori is a major human pathogen causing gastritis, ulcers, and gastric cancers.
- Helicobacter species colonize the upper intestine, contributing to various pathologies.
- Understanding Helicobacter adaptation to bile is crucial for explaining niche colonization.
Purpose of the Study:
- To characterize cell surface proteomic changes in Helicobacter species under bile stress.
- To investigate differential responses to bile stress among various Helicobacter species.
- To establish ProteinChip technology for analyzing Helicobacter proteomics.
Main Methods:
- Surface-enhanced laser desorption/ionization-time of flight mass spectrometry (SELDI-TOF MS) was employed.
- Surface extracts from H. pylori, H. bilis, H. pullorum, and "Helicobacter sp. flexispira" were analyzed.
- Cell surface protein profiles were compared under normal and bile-stressed conditions.
Main Results:
- Two distinct proteomic response patterns to bile stress were identified in vitro.
- H. bilis and H. pullorum showed increased peaks at 7.6 and 7.9 kDa, respectively, under bile stress.
- "Helicobacter sp. flexispira" and H. pylori isolates exhibited decreased low-mass peaks and one induced peak under bile stress.
Conclusions:
- ProteinChip technology is effective for Helicobacter proteomics.
- Different Helicobacter species display unique proteomic responses to bile stress.
- These varied responses may provide insights into Helicobacter niche adaptation and colonization.