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Clostridium perfringens--specific lysin.

S Nakamura, I Okada, J Mizuno

    Canadian Journal of Microbiology
    |May 1, 1977
    PubMed
    Summary
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    A Clostridium perfringens lysate showed lytic activity against many C. perfringens strains and some C. plagarum strains. This specific lysin demonstrated limited activity against other clostridial species.

    Area of Science:

    • Microbiology
    • Bacteriology
    • Enzymology

    Background:

    • Clostridium perfringens is an important bacterial pathogen.
    • Bacteriophages and their derived lysins are explored for antimicrobial applications.

    Purpose of the Study:

    • To characterize a lytic agent derived from Clostridium perfringens strain KZ219.
    • To determine the spectrum of activity and optimal conditions for this lysin.

    Main Methods:

    • Induction of a bacterial lysate from C. perfringens using mitomycin C.
    • Testing the lytic activity of the lysate against various C. perfringens strains and other clostridial species.
    • Assessing the effect of pH, proteolytic enzymes, and heat on lysin activity.

    Main Results:

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    • The lysate was lytic to 50 strains of C. perfringens (types A-E) and 3 strains of C. plagarum.
    • The lysin showed limited activity against only 2 out of 87 strains from 51 other clostridial species.
    • Optimal lytic activity occurred at pH 5.5.
    • Activity was significantly reduced by proteolytic enzymes and heat (60°C for 5 min).

    Conclusions:

    • The induced lysate contains a specific lysin with potent activity against C. perfringens.
    • This lysin exhibits a narrow spectrum of activity, primarily targeting C. perfringens and closely related species.
    • The lytic agent's sensitivity to enzymes and heat suggests a protein-based nature.