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Processing of Clostridium perfringens Enterotoxin by Intestinal Proteases.
Archana Shrestha1, Jessica L Gonzales2, Juliann Beingesser2
1Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, PA USA 15219.
Biorxiv : the Preprint Server for Biology
|February 24, 2025
Summary
Clostridium perfringens enterotoxin (CPE) is processed by intestinal proteases, but this cleavage does not eliminate its ability to form pores and cause food poisoning and diarrhea.
Area of Science:
- Microbiology
- Toxicology
- Gastroenterology
Background:
- Clostridium perfringens type F causes food poisoning and diarrhea.
- Virulence depends on Clostridium perfringens enterotoxin (CPE).
- CPE forms pores in host cell membranes.
Purpose of the Study:
- Investigate the in vitro, ex vivo, and in vivo processing of CPE by intestinal proteases.
- Determine the effects of this processing on CPE activity and enterotoxicity.
Main Methods:
- Purified trypsin and mouse intestinal contents were used to study CPE cleavage.
- Caco-2 cells assessed the activity of processed CPE.
- Mouse small intestinal loops were challenged with CPE to evaluate in vivo effects.
Main Results:
- CPE was rapidly cleaved to a ~32 kDa band by intestinal proteases.
- Processed CPE retained its ability to form large complexes and exhibit cytotoxic activity.
- In vivo, processed CPE still caused intestinal damage, with complexes becoming more stable over time.
Conclusions:
- Intestinal proteases, including trypsin, process CPE.
- Processed CPE remains toxic and enterotoxic, contributing to disease pathogenesis.
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