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Escherichia coli enterotoxin. Purification and partial characterization.

F Dorner

    The Journal of Biological Chemistry
    |November 25, 1975
    PubMed
    Summary
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    Researchers isolated and purified a diarrheagenic protein, enterotoxin, from pathogenic Escherichia coli. This purified enterotoxin induces diarrhea in animal models and affects adenylate cyclase activity.

    Area of Science:

    • Microbiology
    • Biochemistry

    Background:

    • Pathogenic Escherichia coli strains produce enterotoxins that cause diarrhea.
    • Enterotoxins are key virulence factors in bacterial infections.

    Purpose of the Study:

    • To isolate and characterize the enterotoxin from E. coli strain P263.
    • To assess the biological activity of the purified enterotoxin.

    Main Methods:

    • Enterotoxin isolation using Bio-Gel agarose A-5m, Sephadex G-75 chromatography, and preparative isotachophoresis.
    • Purity assessment via immunoelectrophoresis, disc electrophoresis, ultracentrifugation, and immunological assays.
    • Molecular weight determination using gel filtration and SDS-PAGE.
    • Isoelectric point determination.

    Main Results:

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    • A pure enterotoxin was isolated with an apparent molecular weight of 102,000 and an isoelectric point of 6.90.
    • The enterotoxin induced experimental diarrhea in rabbits and piglets.
    • It increased adenylate cyclase activity in cat heart tissue preparations.
    • Enterotoxin activity was acid-labile and destroyed by heating at 65°C for 30 minutes.

    Conclusions:

    • The purified enterotoxin is a potent diarrheagenic agent.
    • The study provides insights into the biochemical properties and biological effects of this E. coli enterotoxin.
    • Heat-stable enterotoxin may result from a complex with endotoxin or capsular material.