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Archives of Microbiology

, Volume 116, Issue 2, pp 119–124 | Cite as

Studies on growth inhibition by lectins of penicillia and aspergilli

  • Rivka Barkai-Golan
  • David Mirelman
  • Nathan Sharon
Article

Abstract

It has previously been shown in our laboratory that wheat germ agglutinin (WGA) binds to Trichoderma viride and inhibits growth of this fungus. Here we report on the effect of WGA, soybean agglutinin (SBA) and peanut agglutinin (PNA) on Penicillia and Aspergilli. Binding of the lectins to the fungi was examined with the aid of their fluorescein isothiocyanate (FITC) conjugated derivatives. FITC-WGA bound to young hyphal walls of all species, in particular to the hyphal tips and septa, in agreement with the chitinous composition of the cell walls of the two genera. Hyphae of all species examined were labelled, though in different patterns, by FITC-SBA and FITC-PNA, suggesting the presence of galactose residues on their surfaces. Young conidiophores, metulae (of the Penicillia), vesicles (of the Aspergilli), sterigmata and young spores, were also labelled. The three lectins inhibited incorporation of [3H]acetate, N-acetyl-D-[3H]glucosamine and D-[14C]galactose into young hyphae of Aspergillus ochraceus, indicating interference with fungal growth. Inhibition of spore germination by the three lectins was also observed. Preincubation of the lectins with their specific saccharide inhibitors prevented binding and the inhibitory effects. We conclude that lectins are useful tools for the study of fungal cell surfaces, and may also serve as an important aid in fungal classification. The present findings also support the suggestion that one role of lectins in plants is protection against fungal pathogens.

Key words

Lectins Fluorescin-conjugated lectins Fungal cell walls Inhibition of fungal growth Penicillium italicum Aspergillus niger Aspergillus flavus Aspergillus ochraceus Stemphylium botryosum Role of lectins in plants 

Abbreviations

Con A

concanavalin A

PNA

peanut agglutinin

SBA

soybean agglutinin

WGA

wheat germ agglutinin

FITC

fluorescein isothiocyanate

GlcNAc

N-acetyl-D-glucosamine

GalNAc

N-acetyl-D-galactosamine

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References

  1. Bardalaye, P. C., Hordin, J. H.: Galactosaminogalactan from cell walls of Aspergillus niger. J. Bacteriol. 125, 655–669 (1976)PubMedGoogle Scholar
  2. Bartnicki-Garcia, S.: Cell wall chemistry, morphogenesis and taxonomy of fungi. Ann. Rev. Microbiol. 22, 87–107 (1968)CrossRefGoogle Scholar
  3. Clark, H. F., Shepard, C. C.: A dialysis technique for preparing fluorescent antibody. Virology 20, 642–644 (1963)PubMedGoogle Scholar
  4. Galun, E.: Morphogenesis in Trichoderma: Autoradiography of intact colonies labelled by [3H]N-acetylglucosamine as a marker of new cell wall biosynthesis. Arch. Mikrobiol. 86, 305–314 (1972)PubMedGoogle Scholar
  5. Galun, M., Braun, A., Frensdorff, A., Galun, E.: Hyphal walls of isolated lichen fungi. Arch. Microbiol. 108, 9–16 (1976)PubMedGoogle Scholar
  6. Gordon, J. A., Blumberg, S., Lis, H., Sharon, N.: Purification of soybean agglutinin by affinity chromatography on Sepharose-N-ε-aminocaproyl-β-D-galactopyranosylamine. FEBS Lett. 24, 193–196 (1972)PubMedGoogle Scholar
  7. Grisaro, V., Sharon, N., Barkai-Golan, R.: The chemical composition of the cell walls of Penicillium digitatum Sacc. and Penicilium italicum Whem. J. gen. Microbiol. 51, 145–150 (1968)PubMedGoogle Scholar
  8. Horikoshi, K., Iida, S.: Studies of the spore coats of fungi I. Isolation and composition of the spore coats of Aspergillus oryzae. Biochim. Biophys. Acta. 83, 197–203 (1964)PubMedGoogle Scholar
  9. Lis, H., Sharon, N.: Lectins: their chemistry and application to immunology. In: The Antigens, Vol. IV (M. Sela, ed.), pp. 429–529. New York: Academic Press 1977Google Scholar
  10. Lotan, R., Gussin, A. E. S., Lis, H., Sharon, N.: Purification of wheat germ agglutinin by affinity chromatography on a Sepharose-bound N-acetylglucosamine derivative. Biochem. Biophys. Res. Commun. 52, 656–662 (1973)PubMedGoogle Scholar
  11. Lotan, R., Skutelsky, E., Danon, D., Sharon, N.: The purification, composition, and specificity of the anti-T lectin from peanut (Arachis hypogaea). J. Biol. Chem. 250, 8518–8523 (1975)PubMedGoogle Scholar
  12. Mirelman, D., Galun, E., Sharon, N., Lotan, R.: Inhibition of fungal growth by wheat germ agglutinin. Nature 256, 414–416 (1975)PubMedGoogle Scholar
  13. Rupley, J. A.: The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular weight substrates for lysozyme. Biochim. Biophys. Acta 83, 243–255 (1964)Google Scholar
  14. Sharon, N., Lis, H.: Lectins: cell-agglutinating and sugar-specific proteins. Science 177, 949–959 (1972)PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Rivka Barkai-Golan
    • 1
  • David Mirelman
    • 1
  • Nathan Sharon
    • 1
  1. 1.Department of BiophysicsThe Weizmann Institute of ScienceRehovothIsrael

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