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SELECTIVE INHIBITION BY TRYPTOPHAN ANALOGUES OF MURINE TOXIN SYNTHESIS IN PASTEURELLA PESTIS

T C MONTIE, S J AJL

    Journal of Bacteriology
    |November 1, 1964
    PubMed

    Insights

    Tryptophan analogues selectively inhibit toxin synthesis in Pasteurella pestis without significantly affecting overall protein production. This suggests cellular tryptophan levels regulate protein quantity and quality.

    Area of Science:

    • Microbiology
    • Biochemistry

    Background:

    • Pasteurella pestis produces toxins crucial for virulence.
    • Tryptophan is an essential amino acid involved in protein synthesis.

    Purpose of the Study:

    • To investigate the effect of tryptophan analogues on toxin synthesis in Pasteurella pestis.
    • To determine if toxin synthesis can be selectively inhibited.

    Main Methods:

    • Washed-cell suspensions of P. pestis were grown in the presence of various tryptophan analogues.
    • Protein synthesis and toxin production were measured.
    • Acrylamide gel electrophoresis was used to analyze protein fractions.

    Main Results:

    • Tryptophan analogues preferentially inhibited toxin synthesis over total protein formation.
    • 5-fluorotryptophan showed growth-inhibitory effects at high concentrations, but toxin production was more sensitive.
    • Inhibition was reversed by l-tryptophan and indole.
    • One toxin-protein band, associated with the cell membrane, was selectively blocked.

    Conclusions:

    • Cellular tryptophan levels influence the quantity and quality of proteins synthesized.
    • Tryptophan analogues offer a potential strategy for selectively inhibiting bacterial toxin production.
    Keywords:
    ANTHRANILIC ACIDELECTROPHORESISEXPERIMENTAL LAB STUDYINDOLESMETABOLISMPASTEURELLA PESTISPHARMACOLOGYPROTEIN METABOLISMSHIKIMIC ACIDTOXINS AND ANTITOXINSTRYPTOPHAN

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