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Updated: Jul 18, 2026
Enrichment and Detection of Clostridium perfringens Toxinotypes in Retail Food Samples
Published on: October 18, 2019
Detection of fibronectin-binding proteins in Clostridium perfringens
Seiichi Katayama1, Nanami Nozu, Masako Yokoyama
1Department of Life Sciences, Okayama University of Science, Okayama 700-0005, Japan. katayama@dbc.ous.ac.jp
Abstract:
Clostridium perfringens is an anaerobic spore-forming pathogen of humans and animals. C. perfringens type A strains, 13, CPN50, and NCTC8237, isolated from human gas gangrene, bound specifically to human fi bronectin (Fn). The trypsin-treatment of the bacterial cells significantly reduced the Fn-binding. A ligand blotting analysis of all three C. perfringens strains revealed that 5 protein bands of 34 kDa, 29 kDa, 26 kDa, 17 kDa, and 12 kDa specifically bound to biotinylated Fn. These results suggest that C. perfringens possesses certain Fn-binding proteins on the cell surface.
Insights
Clostridium perfringens, a gas gangrene pathogen, binds to human fibronectin (Fn). Researchers identified specific fibronectin-binding proteins on the bacterial surface, suggesting their role in infection.
Area of Science:
- Microbiology
- Pathogen Research
- Protein-Ligand Interactions
Background:
- Clostridium perfringens is an anaerobic, spore-forming bacterium known to cause gas gangrene in humans and animals.
- Bacterial adherence to host tissues is a critical step in pathogenesis.
Purpose of the Study:
- To investigate the interaction between Clostridium perfringens type A strains and human fibronectin (Fn).
- To identify potential fibronectin-binding proteins on the surface of C. perfringens.
Main Methods:
- Culturing and isolation of C. perfringens type A strains (13, CPN50, NCTC8237) from human gas gangrene cases.
- Assessing bacterial binding to human fibronectin.
- Trypsin treatment of bacterial cells to evaluate the role of surface proteins in Fn-binding.
- Ligand blotting analysis using biotinylated Fn to identify specific binding proteins.
Main Results:
- C. perfringens type A strains demonstrated specific binding to human fibronectin.
- Trypsin treatment significantly reduced fibronectin binding, indicating protein involvement.
- Ligand blotting identified five bacterial protein bands (34, 29, 26, 17, and 12 kDa) that specifically bound fibronectin.
Conclusions:
- Clostridium perfringens possesses surface proteins that bind to human fibronectin.
- These fibronectin-binding proteins may play a role in the adherence and pathogenesis of C. perfringens infections like gas gangrene.
