1887

Abstract

The mode of transport of the complex toxin molecule of (which has a mol. wt of 84000 and consists of several subunits) across the inner and outer membranes of is not known. In this study we found two peptides in the outer and inner membranes of which may be the form in which the toxin subunits are transported across the membrane. We examined two growth conditions: aerobic growth at 37 °C, when most of the synthesized toxin is membrane-bound; and anaerobic growth at 37 °C, when little toxin remains membrane-bound, the toxin being released into the growth medium. When was grown aerobically at 37 °C, the outer and the inner membranes contained two peptides with mol. wts of approximately 22000 and 6000 which were not found in the outer or the inner membrane of anaerobically grown cells. Sodium deoxycholate, which releases membrane-bound toxin, released several peptides including the 22000 and the 6000 mol. wt peptides. Trypsin also released the 22000 and 6000 mol. wt peptides. Purified cholera toxin had three kinds of peptides, of mol. wt 21000 (A peptide), 11000 (B subunit) and 5000 (A peptide). We postulate that the membrane peptides may be precursors of the A subunit of the toxin molecule.

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/content/journal/micro/10.1099/00221287-103-2-381
1977-12-01
2021-05-15
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References

  1. Ames G. F. 1974; Resolution of bacterial proteins by polyacrylamide gel electrophoresis. Journal of Biological Chemistry 249:634–644
    [Google Scholar]
  2. Callahan L. T., Richardson S. H. 1973; Biochemistry of Vibrio cholerae virulence. III. Nutritional requirements for toxin production and the effect of pH on toxin elaboration in chemically defined media. Infection and Immunity 7:567–572
    [Google Scholar]
  3. Fernandes P. B., Smith H. L. 1977; The effect of anaerobiosis and bile salts on the growth and toxin production by Vibrio cholerae. Journal of General Microbiology 98:77–86
    [Google Scholar]
  4. Fernandes P. B., Clark J. M., Smith H. L. 1977; Morphology of Vibrio cholerae during enterotoxin production under anaerobic conditions. Journal of Ultrastructure Research 58:252–260
    [Google Scholar]
  5. Finkelstein R. A. 1975; Cholera enterotoxin. In Microbiology - 1975 pp. 236–241 Schlessinger D. Edited by Washington: American Society for Microbiology.;
    [Google Scholar]
  6. Finkelstein R. A., Peterson J. W., Lospalluto J. J. 1971; Conversion of cholera exo-enterotoxin (choleragen) to natural toxoid (choleragenoid). Journal of Immunology 106:868–871
    [Google Scholar]
  7. Holmgren J., Lönnroth I., Svennerholm L. 1973; Tissue receptor for cholera exotoxin: postulated structure from studies with GM1 ganglioside and related glycolipids. Infection and Immunity 8:208–214
    [Google Scholar]
  8. Inouye M., Yee M. 1972; Specific removal of proteins from the envelope of Escherichia coli by protease treatments. Journal of Bacteriology 112:585–592
    [Google Scholar]
  9. Laemmli U. K., Favre M. 1973; Maturation of the head of bacteriophage T4.1. DNA packaging events. Journal of Molecular Biology 80:575–599
    [Google Scholar]
  10. Lampen J. O. 1974; Movement of extracellular enzymes across cell membranes. Symposia of the Society for Experimental Biology 28:351–374
    [Google Scholar]
  11. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  12. Lugtenberg B., Peters R., Bernheimer H., Berendsen W. 1976; Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli. Molecular and General Genetics 147:251–262
    [Google Scholar]
  13. Osborn M. J., Gander J. E., Parisi E., Carson J. 1972; Mechanism of assembly of the outer membrane of Salmonella typhimurium. Journal of Biological Chemistry 247:3962–3972
    [Google Scholar]
  14. Rosenbusch J. P. 1974; Characterization of the major envelope protein from Escherichia coli: regular arrangement on the peptidoglycan and unusual sodium dodecyl sulfate binding. Journal of Biological Chemistry 249:8019–8029
    [Google Scholar]
  15. Schnaitman C. 1971; Effect of ethylenediamine- tetraacetic acid, Triton X-100, and lysozyme on the morphology and clinical composition of the cell wall of Escherichia coli. Journal of Bacteriology 108:553–563
    [Google Scholar]
  16. Schneider D., Parker C. 1975; Protease mutants of Vibrio cholerae. In Proceedings of the Eleventh Joint Conference on Cholera pp. 127–133
    [Google Scholar]
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