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pH-dependent binding of Helicobacter pylori to pig gastric mucins
H Nordman1, T Borén, J R Davies
1Mucosal Biology Group, CMB, Lund University, Sweden.
Abstract:
A microtiter-based assay was developed to study the binding of Helicobacter pylori to pig gastric mucins purified by density-gradient centrifugation in CsCl/4 M guanidinium chloride. Binding of H. pylori was observed over the 'mucin' band as well as with 'low-density' components in the gradients, and binding to the latter was more pronounced when incubations were performed at 37 degrees C as compared to 20 degrees C. At a lower pH, binding of H. pylori (strain SVA 40) to the 'high-density' mucins from pig antrum was increased but binding to the 'low-density' ones was decreased. Binding of the P466 strain (Le(b)-specific) was mainly associated with the 'mucin' band, whereas the MO19 strain reacted preferentially with the 'low-density' components. In summary, H. pylori may bind to gastric mucins and the binding is influenced by temperature, pH and the repertoire of bacterial adhesins.
Insights
Helicobacter pylori binds to pig gastric mucins, with binding influenced by temperature, pH, and bacterial adhesins. Different bacterial strains show varied binding preferences to mucin components.
Area of Science:
- Microbiology
- Gastroenterology
- Biochemistry
Background:
- Helicobacter pylori is a significant pathogen causing gastric diseases.
- Gastric mucins form a protective layer in the stomach, crucial for host-pathogen interactions.
- Understanding H. pylori adhesion mechanisms is vital for developing therapeutic strategies.
Purpose of the Study:
- To develop and utilize a microtiter-based assay for studying H. pylori binding to pig gastric mucins.
- To investigate the influence of temperature, pH, and bacterial strain on H. pylori-mucin interactions.
Main Methods:
- Purification of pig gastric mucins using density-gradient centrifugation (CsCl/4 M guanidinium chloride).
- Development of a microtiter-based assay to quantify H. pylori binding to purified mucins.
- Analysis of binding patterns under varying temperature (20°C vs. 37°C) and pH conditions.
Main Results:
- H. pylori binding occurred with both 'mucin' bands and 'low-density' components.
- Binding to low-density components was enhanced at 37°C compared to 20°C.
- Lower pH increased binding to high-density mucins but decreased binding to low-density components.
- Specific H. pylori strains (P466, MO19) exhibited distinct binding preferences for mucin fractions.
Conclusions:
- H. pylori adheres to gastric mucins through interactions influenced by environmental factors.
- Temperature and pH significantly modulate the binding affinity of H. pylori to different mucin components.
- Bacterial adhesin profiles dictate strain-specific binding patterns to gastric mucins, highlighting the complexity of host colonization.