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Interaction of Campylobacter jejuni with extracellular matrix components
Biochimica Et Biophysica Acta
|December 8, 1989
Summary
Campylobacter jejuni uses extracellular matrix components like fibronectin and collagens for adhesion. Different bacterial strains show varied binding capacities, indicating multiple attachment mechanisms.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- Campylobacter jejuni is a leading cause of bacterial gastroenteritis worldwide.
- Bacterial adhesion to host tissues is a critical step in pathogenesis.
- Extracellular matrix (ECM) proteins are abundant in host tissues and can mediate bacterial attachment.
Purpose of the Study:
- To investigate the role of specific ECM components in Campylobacter jejuni adhesion.
- To determine if different strains of C. jejuni exhibit distinct binding preferences for ECM proteins.
Main Methods:
- Adhesion assays were performed using three strains of C. jejuni.
- Coverslips and microwells were coated with purified ECM components: fibronectin, laminin, and types I, III, IV, and V collagens.
- Bacterial attachment was quantified after incubation with coated surfaces.
Main Results:
- Fibronectin significantly mediated C. jejuni adherence, with strain-specific differences observed.
- Types I, III, and V collagens strongly promoted the attachment of two C. jejuni strains.
- All strains showed weak attachment to type IV collagen, while laminin mediated adhesion only at higher concentrations.
Conclusions:
- ECM components, including fibronectin and various collagens, act as crucial anchor molecules for C. jejuni.
- Multiple simultaneous attachment mechanisms are involved in C. jejuni adhesion to host surfaces.
- Understanding these interactions can inform strategies to control C. jejuni infections.
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