The Spontaneous Release of Somatic Antigen from Free

Abstract

SUMMARY: Culture supernatants of Ogawa and Inaba strains of contained somatic antigen, judging by their ability to inhibit the vibriocidal action of homologous antisera. Antigen was readily detectable during the exponential phase of growth. The release of antigen was not entirely dependent on cell lysis or death, nor was the decrease in the pH of the medium during the early phase of growth responsible for antigen release. As the concentration of antigen increased, protein, carbohydrate and 260 nm-absorbing material increased in dialysed supernatants but an intracellular enzyme, malate dehydrogenase, was not detectable up to 40 h growth. The antigen demonstrable in supernatants at 40 h accounted for more than a third of the total capacity of the cultures to inhibit vibriocidal antibody. Ethylenediaminetetra-acetate not only increased the release of antigen in suspensions of agar-grown vibrios but also released intracellular substances. Supernatants of Ogawa cultures were distinctly more inhibitory than Inaba supernatants but both were equally effective in gel diffusion precipitation.

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1974-03-01
2024-03-28
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References

  1. Dubois M., Gilles K. A., Hamilton J. K., Rebers P. A., Smith F. 1956; Colorimetric method for determination of sugars and related substances. Analytical Chemistry 28:350–356
    [Google Scholar]
  2. Eagon R. G., Carson K. J. 1965; Lysis of cell walls and intact cells of Pseudomonas aeruginosa by ethylenediaminetetra acetic acid and by lysozyme. Canadian Journal of Microbiology 11:193–201
    [Google Scholar]
  3. Finkelstein R. A. 1962; Vibriocidal antibody inhibition (VAI) analysis: a technique for the identification of the predominant vibriocidal antibodies in serum and for the detection and identification of Vibrio cholerae antigens. Journal of Immunology 89:264–271
    [Google Scholar]
  4. Finkelstein R. A., Atthasampunna P., Chulasamaya M., Charunmethee P. 1966; Pathogenesis of experimental cholera: biologic activities of purified procholeragen A. Journal of Immunology 96:440–449
    [Google Scholar]
  5. Finkelstein R. A., Norris H. T., Dutta N. K. 1964; Pathogenesis of experimental cholera in infant rabbits. I. Observations on the intraintestinal infection and experimental cholera produced with cell- free products. Journal of Infectious Diseases 114:203–216
    [Google Scholar]
  6. Gallut J. 1962; Contribution a l’étude du complexe antigènique ‘O’ des vibrions. Annales de l’Institut Pasteur 102:309–327
    [Google Scholar]
  7. Holmgren J., Lönnroth I., Ouchterlony Ö. 1971; Immunochemical studies of two cholera toxin- containing standard culture filtrate preparations of Vibrio cholerae . Infection and Immunity 3:747–755
    [Google Scholar]
  8. Kaur J., Shrivastav J. B. 1964; Immunochemical studies in vibrio polysaccharides. Indian Journal of Medical Research 52:809–816
    [Google Scholar]
  9. Leive L., Shovlin V. K., Mergenhagen S. E. 1968; Physical, chemical and immunological properties of lipopolysaccharide released from Escherichia coli by ethylenediaminetetraacetate. Journal of Biological Chemistry 243:6384–6391
    [Google Scholar]
  10. 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]
  11. Milner K. C., Rudbach J. A., Ribi E. 1971; General characteristics. In Microbial Toxins 4 Bacterial Endotoxins pp. 1–65 Weinbaum G., Kadis S., Ajl S. J. Edited by New York and London: Academic Press;
    [Google Scholar]
  12. Neoh S. H., Rowley D. 1970; The antigens of Vibrio cholerae involved in the vibriocidal action of antibody and complement. Journal of Infectious Diseases 121:505–513
    [Google Scholar]
  13. Nilsson L. A. 1968; Comparative testing of precipitation methods for quantitation of C-reactive protein in blood serum. Acta pathologica et microbiologica scandinavica 73:129–144
    [Google Scholar]
  14. Pike R. M., Chandler C. H. 1969; Agglutinating and bactericidal properties of fractions of rabbit anti-Vibrio cholerae serum. Infection and Immunity 98:956–962
    [Google Scholar]
  15. Repaske R. 1958; Lysis of Gram-negative organisms and the role of Versene. Biochimica et biophysica acta 30:225–232
    [Google Scholar]
  16. Verwey W. F., Watanabe Y., Phillips P. E., Williams H. R. Jun 1965; The partial purification and some of the properties of the mouse protective antigen of the Inaba subtype of Vibrio cholerae (El Tor). In Proceedings of the Cholera Research Symposium, January 24-29, 1965, Honolulu, Hawaii U.S. Public Health Service Publication no. 1328 pp. 259–263 Washington: U.S. Government Printing Office;
    [Google Scholar]
  17. Watanabe Y., Verwey W. F. 1965; Protective antigens from El Tor vibrios. Bulletin of the World Health Organization 32:809–821
    [Google Scholar]
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