1887

Abstract

SUMMARY

Alpha toxin purified from strain Wood 46 and radioiodinated by the lactoperoxidase method retained full haemolytic activity and was used to study factors affecting binding to rabbit and horse erythrocytes. A relatively fixed percentage of added toxin bound to both cell types; the percentage bound was independent of temperature, H, cell concentration and toxin concentration. Neither a 50-fold excess of native toxin nor Concanavalin A inhibited the binding of iodinated toxin to erythrocytes. The results suggest that differences in the sensitivity of erythrocytes to haemolysis do not reflect the abundance of high affinity toxin receptors on sensitive cells, but are more probably the result of differences in the intrinsic stability of the membrane and its sensitivity to perturbation by amphiphilic agents.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-18-2-197
1984-10-01
2022-11-29
Loading full text...

Full text loading...

/deliver/fulltext/jmm/18/2/medmicro-18-2-197.html?itemId=/content/journal/jmm/10.1099/00222615-18-2-197&mimeType=html&fmt=ahah

References

  1. Arbuthnott J. P., Freer J. H., Billcliffe B. 1973; Lipid-induced polymerization of staphyloccal α-toxin. Journal of General Microbiology 75:309–319
    [Google Scholar]
  2. Barei G. M., Fackrell H. B. 1979; The binding of fluorescein-labelled staphylococcal alpha toxoid to erythrocytes. Canadian Journal of Microbiology 25:1219–1226
    [Google Scholar]
  3. Benheimer A. W. 1974; Interactions between membranes and cytolytic bacterial toxins. Biochimica et Biophysica Acta 344:27–50
    [Google Scholar]
  4. Bernheimer A. W., Avigad L. S. 1980; Inhibition of bacterial and other cytolysins by glycophorin. FEMS Microbiology Letters 9:15–17
    [Google Scholar]
  5. Bernheimer A. W., Schwartz L. L. 1963; Isolation and composition of staphylococcal alpha toxin. Journal of General Microbiology 30:455–468
    [Google Scholar]
  6. Bhakdi S., Fussle R., Tranum-Jensen J. 1981; Staphyloccal α-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles. Proceedings of the National Academy of Science (USA) 78:5475–5479
    [Google Scholar]
  7. Birkbeck T. H., Chao L.-P., Arbuthnott J. P. 1974; Sensitivity of erythrocytes of marine fish to staphylococcal delta haemolysin. Proceedings of the Society for General Microbiology 1:55
    [Google Scholar]
  8. Bretscher M. S. 1973; Membrane structure: some general principles. Science 181:622–629
    [Google Scholar]
  9. Cassidy P. S., Harshman S. 1973; The binding of staphylococcal 125I-α-toxin (B) to erythrocytes. Journal of Biological Chemistry 248:5545–5546
    [Google Scholar]
  10. Cassidy P., Harshman S. 1976a; Studies on the binding of staphylococcal 125I labeled α-toxin to rabbit erythrocytes. Biochemistry 15:2348–2355
    [Google Scholar]
  11. Cassidy P., Harshman S. 1976b; Purification of staphylococcal alpha-toxin by adsorption chromatography on glass. Infection and Immunity 13:982–986
    [Google Scholar]
  12. Cassidy P., Harshman S. 1979; Characterization of detergent-solubilized iodine-125-labeled α-toxin bound to rabbit erythrocytes and mouse diaphragm muscle. Biochemistry 18:232–236
    [Google Scholar]
  13. Chao L.-P., Birkbeck T. H. 1978; Assay of staphylococcal δ-haemolysin with fish erythrocytes. Journal of Medical Microbiology 11:303–313
    [Google Scholar]
  14. Cooper L. Z., Madoff M. A., Weinstein L. 1966; Heat stability and species range of purified staphylococcal α-toxin. Journal of Bacteriology 91:1686–1692
    [Google Scholar]
  15. Dalen A. B. 1976; Proteolytic degradation of staphylococcal α-toxin. Acta Pathologica et Microbiologica Scandinavica B84:309–314
    [Google Scholar]
  16. England B. J., Gunn R. B., Steck T. L. 1980; An immunological study of band 3, the anion transport protein of the human red blood cell membrane. Biochimica et Biophysica Acta 623:171–182
    [Google Scholar]
  17. Freer J. H. 1982; Cytolytic toxins and surface activity. Toxicon 20:217–221
    [Google Scholar]
  18. Freer J. H., Arbuthnott J. P., Bernheimer A. W. 1968; Interaction of staphylococcal α-toxin with artificial and natural membranes. Journal of Bacteriology 95:1153–1168
    [Google Scholar]
  19. Freer J. H., Arbuthnott J. P., Billcliffe B. 1973; Effects of staphyloccal α-toxin on the structure of erythrocyte membranes: a biochemical and freeze-etching study. Journal of General Microbiology 75:321–332
    [Google Scholar]
  20. Füssle R., Bhakdi S., Sziegoleit A., Tranum-Jensen J., Kranz T., Wellensiek H.-J. 1981; On the mechanism of membrane damage by Staphylococcus aureus α-toxin. Journal of Cell Biology 91:83–94
    [Google Scholar]
  21. Hubbard A. L., Cohn Z. A. 1972; The enzymatic iodination of the red cell membrane. Journal of Cell Biology 55:390–405
    [Google Scholar]
  22. Inoue M., Mori M., Seno S., Utsumi K., Yasuda T. 1974; Structural difference in sites on surface membrane of mature and immature erythrocytes. Nature 250:247–248
    [Google Scholar]
  23. Inoue M., Okajima K., Ito K., Utsumi K., Seno S. 1977; Changes in structural organization of surface membrane during erythrocyte maturation. Biochimica et Biophysica Acta 467:130–136
    [Google Scholar]
  24. Kato I., Sakoda K., Saito M., Suzuki Y., Watanabe M. 1975a; Studies on the haemolytic action of staphylococcal alpha toxin. Japanese Journal of Medical Science and Biology 28:332–334
    [Google Scholar]
  25. Kato I., Sakoda K., Saito M., Suzuki Y., Watanabe M. 1975b; Inhibitory effect of flavin mononucleotide on the hemolysis of rabbit erythrocytes by staphylococcal alpha-toxin. Infection and Immunity 12:696–697
    [Google Scholar]
  26. Kato I., Sakoda K., Saito M., Suzuki Y. 1977; Effects of lectins on the haemolysis of rabbit erythrocytes by staphylococcal alpha toxin. Microbiology and Immunology 21:517–524
    [Google Scholar]
  27. Kimelberg H. K., Papahadjopoulos D. 1971; Phospholipid-protein interactions: membrane permeability correlated with monolayer “penetration”. Biochimica et Biophysica Acta 233:805–809
    [Google Scholar]
  28. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
    [Google Scholar]
  29. Lo C. Y., Fackrell H. B. 1979; Immunologic evidence that staphylococcal alpha toxin is oriented on membranes. Canadian Journal of Microbiology 25:686–692
    [Google Scholar]
  30. Lominski I., Arbuthnott J. P. 1962; Some characteristics of staphylococcus α-haemolysin. Journal of Pathology 83:515–520
    [Google Scholar]
  31. Low D. K. R., Freer J. H., Arbuthnott J. P., Möllby R., Wadstrom T. 1974; Consequences of sphingomyelin degradation in erythrocyte ghost membrane by staphylococcal β-toxin (sphingomyelinase C). Toxicon 12:279–285
    [Google Scholar]
  32. Maharaj I., Fackrell H. B. 1980; Rabbit erythrocyte band 3,a receptor for staphylococcal alpha toxin. Canadian Journal of Microbiology 26:524–531
    [Google Scholar]
  33. Reisfeld R. A., Lewis U. J., Williams D. E. 1962; Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 195:281–283
    [Google Scholar]
  34. Skutelsky E., Lotan R., Sharon N., Danon D. 1977; Distribution of the T-antigen on erythroid cell surfaces. Studies with peanut agglutinin, an anti-T specific lectin. Biochimica et Biophysica Acta 467:165–174
    [Google Scholar]
  35. Tomarelli R. M., Charney J., Harding M. L. 1949; The use of azoalbumin as a substrate in the colorimetric determination of peptic and tryptic activity. Journal of Laboratory and Clinical Medicine 34:428–433
    [Google Scholar]
  36. Weber K., Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-18-2-197
Loading
/content/journal/jmm/10.1099/00222615-18-2-197
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error