Skip to main content
Log in

δ-Toxin, unlike melittin, has only hemolytic activity and no antimicrobial activity: Rationalization of this specific biological activity

  • Short Papers
  • Published:
Bioscience Reports

Abstract

The antimicrobial activity of a synthetic peptide corresponding to δ-hemolysin had been examined. The peptide didnot exhibit antimicrobial activity against gram negative and gram positive micro-organisms unlike other hemolytic peptides like melittin. This lack of antibacterial activity arises due to the inability of δ-hemolysin to perturb the negatively charged bacterial cell surface and permeabilize the bacterial plasma membrane. However, the red blood cell surface has a structure considerably different from bacteria, and does not act as a barrier to molecules reaching the lipid membrane. Hence δ-toxin can lyse erythrocytes. Thus, the specificity in biological activity has been rationalized in terms of differences, in the interaction of the toxin with the bacterial and red blood cell surfaces.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

References

  1. Bernheimer, A. W. and Rudy, B. (1988)Biochim. Biophys. Acta 864:123–141.

    Google Scholar 

  2. Boman, H. G. (1991)Cell 65:205–207.

    PubMed  Google Scholar 

  3. Zasloff, M. (1987)Proc. Natl. Acad. Sci. USA 84:5449–5453.

    PubMed  Google Scholar 

  4. Lehrer, R. I., Ganz, T. and Selsted, M. E. (1991)Cell 64:229–230.

    PubMed  Google Scholar 

  5. Reddy, E. S. P. and Bhargava, P. M. (1979)Nature 279:725–728.

    PubMed  Google Scholar 

  6. Andreu, D., Merrifield, R. B., Steiner, H. and Boman, H. G. (1985)Biochemistry 24:1683–1688.

    PubMed  Google Scholar 

  7. Zasloff, M., Martin, B. and Chen, H. C. (1988)Proc. Natl. Acad. Sci. USA 85:910–913.

    PubMed  Google Scholar 

  8. Chen, H.-C., Brown, J. H., Morell, J. L. and Huang, C. M. (1988)FEBS Lett. 236:462–466.

    PubMed  Google Scholar 

  9. Boman, H. G., Wade, D., Boman, I. A., Wahlin, B. and Merrifield, R. B. (1989)FEBS Lett. 259:103–106.

    PubMed  Google Scholar 

  10. Andreu, D., Ulbach, J., Boman, A., Wahlin, B., Wade, D., Merrifield, R. B. and Boman, H. G. (1992) FEBS Lett.296:190–194.

    PubMed  Google Scholar 

  11. Fitton, J. E., Dell, A. and Shaw, W. V. (1980)FEBS Lett. 115:209–212.

    PubMed  Google Scholar 

  12. Freer, J. H. and Arbuthnott, J. P. (1983)Pharmacol and Ther.19:55–106.

    Google Scholar 

  13. Thelestam, M. (1983) inStaphylococci and Staphylococcal Diseases (Easmon, C. S. F. and Adlam eds.) Vol. 2, Academic Press, London. pp. 705–774.

    Google Scholar 

  14. Yianni, Y. P., Fitton, J. E. and Morgan, C. G. (1986)Biochim. Biophys. Acta 856: 91–96.

    PubMed  Google Scholar 

  15. Bhakoo, M., Birkbeck, T. H. and Freer, J. H. (1982)Biochemistry 21:6879–6883.

    PubMed  Google Scholar 

  16. Mellor, I. R., Thomas, D. H. and Sansom, M. S. P. (1988)Biochim. Biophys. Acta 942: 280–294.

    PubMed  Google Scholar 

  17. Atherton, E. and Sheppard, R. C.Solid Phase Peptide Synthesis. A Practical Approach, 1989, IRL, Oxford.

    Google Scholar 

  18. Bodanszky, M. and Bodanszky, A. (1984)Int. J. Pept. Protein Res. 23:287–291.

    Google Scholar 

  19. Nagaraj, T., Joseph, M. and Reddy, G. L. (1987)Biochim. Biophys. Acta 903:465–472.

    PubMed  Google Scholar 

  20. Saberwal, G. and Nagaraj, R. (1989)Biochim. Biophys. Acta,984:360–364.

    PubMed  Google Scholar 

  21. Thiaudiere, E., Siffert, O., Talbot, J. C., Bolard, J., Alouf, J. E. and Dufourcq, J. (1991)Eur. J. Biochem. 195:203–213.

    PubMed  Google Scholar 

  22. Alouf, J. E., Dufourcq, J., Siffert, O., Thiaudiere, E. and Geoffroy, C. (1989)Eur. J. Biochem. 183:381–390.

    PubMed  Google Scholar 

  23. Raghunathan, G., Seetharamulu, P., Brooks, B. R. and Guy, H. R. (1990)Proteins 8:231–225.

    Google Scholar 

  24. Lutenberg, B. and van Alphen, L. (1983)Biochim. Biophys. Acta 737:51–115.

    PubMed  Google Scholar 

  25. Strom, D. R., Rosenthal, K. S. and Swanson P. E. (1977)Annu. Rev. Biochem. 46: 723–763.

    PubMed  Google Scholar 

  26. Hammonds S. M., Lambert, P. A. and Rycroft, A. N.The Bacterial Cell Surface, 1984, Croom Helm, London.

    Google Scholar 

  27. Vitala, J. and Jarnefelt, J. (1985)Trends Biochem. Sci. 10:392–395.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Dhople, V.M., Nagaraj, R. δ-Toxin, unlike melittin, has only hemolytic activity and no antimicrobial activity: Rationalization of this specific biological activity. Biosci Rep 13, 245–250 (1993). https://doi.org/10.1007/BF01123506

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01123506

Key Words

Navigation