Skip to main content
Log in

Plant chitinases are potent inhibitors of fungal growth

  • Letter
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

The antimicrobial arsenal of plants is thought to consist mainly of secondary metabolites, among which the phytoalexins are the best-studied1–3. But plants may also possess antimicrobial proteins4,5: it has been reported that wheat-germ agglutinin, a chitin-binding lectin from wheat embryos, inhibits growth of the fungus Trichoderma viride4. This has led to the notion that plant lectins, with their intriguing biochemical similarity to animal antibodies, have an antibody-like antimicrobial function4,6,7. We report here that the main proteinaceous inhibitor of fungal growth in bean leaves is chitinase, an enzyme that can be induced by the plant hormone ethylene, or by pathogen attack. Among commercial preparations of purified chitin-binding lectins (from wheat germ, tomato, potato, pokeweed and gorse), only those containing contaminating chitinase activity inhibit fungal growth. Our data indicate that plant chitinases, but not chitin-binding lectins, are important antifungal proteins in plants.

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.

Similar content being viewed by others

References

  1. Bell, A. A. A. Rev. Pl. Physiol. 32, 22–81 (1981).

    Article  Google Scholar 

  2. Bailey, J. A. & Mansfield, J. W. (eds) Phytoalexins (Halsted, Wiley, New York, 1982).

    Google Scholar 

  3. Darvill, A. G. & Albersheim, P. A. Rev. Pl. Physiol. 35, 243–275 (1984).

    Article  CAS  Google Scholar 

  4. Mirelman, D., Galun, E., Sharon, N. & Lotan, R. Nature 256, 414–416 (1975).

    Article  ADS  CAS  Google Scholar 

  5. Roberts, W. K. & Selitrennikoff, C. P. Biochim. Biophys. Acta 880, 161–170 (1986).

    Article  CAS  Google Scholar 

  6. Sequeira, L. A. Rev. Phytopathol. 16, 453–481 (1978).

    Article  CAS  Google Scholar 

  7. Etzler, M. E. A. Rev. Pl. Physiol. 36, 209–234 (1985).

    Article  CAS  Google Scholar 

  8. Barkai-Golan, R., Mirelman, D. & Sharon, N. Archs. Microbiol. 116, 119–124 (1978).

    Article  CAS  Google Scholar 

  9. Brambl, R. & Gade, W. Physiologia Pl. 64, 402–408 (1985).

    Article  Google Scholar 

  10. Boller, T. in Cellular and Molecular Biology of Plant Stress (eds J. L. Key & T. Kosuge), 247–262 (Liss, New York, 1985).

    Google Scholar 

  11. Molano, J., Polacheck, I., Duran, A. & Cabib, E. J. biol. Chem. 254, 4901–4907 (1979).

    CAS  PubMed  Google Scholar 

  12. Pegg, G. F. & Young, D. H. Physiol. Pl. Pathol. 21, 389–409 (1982).

    Article  CAS  Google Scholar 

  13. Boller, T., Gehri, A., Mauch, F. & Vögeli, U. Planta 157, 22–31 (1983).

    Article  CAS  Google Scholar 

  14. Mauch, F., Hadwiger, L. A. & Boller, T. Pl. Physiol. 76, 607–611 (1984).

    Article  CAS  Google Scholar 

  15. Métraux, J. P. & Boller, T. Physiol. molec. Pl. Pathol. 28, 161–169 (1986).

    Article  Google Scholar 

  16. Bloch, R. & Burger, M. M. Biochem. biophys. Res. Commun. 58, 13–19 (1974).

    Article  CAS  Google Scholar 

  17. Farkas, V. Microbiol. Rev. 43, 117–144 (1979).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Schlumbaum, A., Mauch, F., Vögeli, U. et al. Plant chitinases are potent inhibitors of fungal growth. Nature 324, 365–367 (1986). https://doi.org/10.1038/324365a0

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1038/324365a0

  • Springer Nature Limited

This article is cited by

Navigation