Several chitin-binding proteins were isolated from the “bottom fraction” of Hevea brasiliensis (Müll.) Arg. latex. One of these chitin-binding proteins is hevein, a small monomeric protein which strongly resembles the lectin from stinging nettle (Urtica dioica L.). Like the latter, hevein showed strong antifungal activity against several fungi in vitro. The possible involvement of this protein in the defense against invasion by potentially pathogenic fungi is discussed.
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fast protein liquid chromatography
- Mr :
apparent molecular mass
Sodium dodecyl sulp-hatepolyacrylamide gel electrophoresis
Urtica dioica agglutinin
Ansari, A.A., Mage, R.G. (1976) An evaluation of effectiveness of bio glass in molecular sieving of polypeptides in guanidine hydrochloride. Anal. Biochem. 74, 118–125
Archer, B.L. (1960) The proteins of Hevea brasiliensis latex. 4. Isolation and characterization of crystalline hevein. Biochem. J. 75, 236–240
Archer, B.L., Audley, B.G., Sweeney, G.P., Tan, Chee Hong (1969) Studies on composition of latex serum and ‘bottom fraction’ particles. J. Rubber Res. Inst. Malays. 21, 560–569
Boller, T. (1988) Ethylene and the regulation of antifungal hydrolases in plants. In: Oxford surveys of plant molecular and cell biology, vol. 5, pp. 145–174, Miflin, B.J., ed. Oxford University Press, Oxford
Boller, T., Kende, H. (1979) Hydrolytic enzymes in the central vacuole of plant cells. Plant Physiol. 63, 1123–1132
Broekaert, W.F. (1988) Chitinases and chitin-binding lectins in plants: a biochemical and physiological study of their role in the natural protection of plants against fungi. Dissertationes de agricultura 165, Fakulteit Landbouw-wetenschappen, K.U. Leuven
Broekaert, W.F., Van Parijs, J., Allen, A.K., Peumans, W.J. (1988) Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat. Physiol. Mol. Plant Pathol. 33, 319–331
Broekaert, W.F., Van Parijs, J., Leyns, F., Joos, H., Peumans, W.J. (1989) A chitin-binding lectin from stinging nettle rhizomes with antifungal properties. Science 245, 1100–1102
Cabib, E. (1987) The synthesis and degradation of chitin. Adv. Enzymol. 59, 59–101
Chapot, M.P., Peumans, W.J., Strosberg, A.D. (1986) Extensive homologies between lectins from non-leguminous plants. FEBS Lett. 195, 231–234
Jollés, P. (1962) Lysosomes from rabbit spleen and dog spleen. In: Methods in enzymology, vol. V, pp. 137–140, Colowick, S.P., Kaplan, N.O., eds. Academic Press, New York London
Kocourek, J., Horejsi, V. (1981) Defining a lectin. Nature 290, 188
Koop, D.R., Morgan, E.T., Tarr, G.E., Coon, M.U. (1982) Purification and characterization of a unique isozyme of cytochrome from liver microsomes of ethanol-treated rabbits. J. Biol. Chem. 257, 8472–8480
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277, 680–685
Mauch, F., Staehelin, L.A. (1989) Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant Cell 1, 447–457
Mauch, F., Mauch-Mani, B., Boller, T. (1988) Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase. Plant Physiol. 88, 936–942
Mirelman, D., Galun, E., Sharon, N., Lotan, R. (1975) Inhibition of fungal growth by wheat germ agglutinin. Nature 256, 414–416
Peumans, W.J., Stinissen, H.M., Carlier, A.R. (1982) Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale reale) and barley (Hordeum vulgare) embryos. Biochem J. 203, 239–243
Peumans, W.J., De Ley, M., Broekaert, W.F. (1983) An unusual lectin from stinging nettle (Urtica dioica) rhizomes. FEBS Lett. 177, 99–103
Price, J.S., Storck, R. (1975) Production, purification and characterization of an extracellular chitosanase from Streptomyces. J. Bacteriol. 124, 1574–1585
Rupley, J.A. (1964) The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular-weight substrates for lysozyme. Biochim. Biophys. Acta 29, 522–534
Schlumbaum, A., Mauch, F., Voegeli, V., Boller, T. (1986) Plant chitinases are potent inhibitors of fungal growth. Nature 324, 365–367
Tata, S.J. (1975) Hevein: its isolation, purification and some structural aspects. In: Proc. Int. Rubber Conference, Kuala Lumpur, vol II, pp. 499–517, Rubber Res. Inst. Malaysia, Kuala Lumpur
Tata, S.J., Beintema, J.J., Balabaskaran, S. (1983) The lysozyme of Hevea brasiliensis latex: isolation, purification, enzyme kinetics and a partial amino acid sequence. J. Rubber Res. Inst. Malays. 31, 35–42
Walsh, K.A. (1970) Trypsinogens and trypsins of various species. In: Methods of enzymology, vol XIV, pp. 41–63, Perlmann, G.E., Lorand, L., eds. Academic Press, New York, London
Walujono, K., Scholma, R.A., Beintema, J.J., Mariono, A., Hahn, A.M. (1975) Amino acid sequence of hevein. In: Proc. Int. Rubber Conference, Kuala Lumpur, vol II, pp. 518–531, Rubber Res. Inst. Malaysia, Kuala Lumpur
Wessels, J.G.H. (1988) A steady-state model for apical wall growth in fungi. Acta Bot. Neerl. 37, 3–16
Wright, H.T., Brooks, D.M., Wright, C.S. (1985) Evolution of the multidomain protein wheat germ agglutinin. J. Mol. Evol. 21, 133–138
This work is supported in part by NIH grant and grants of the National Fund for Scientific Research (Belgium): W.J.P. is senior research associate, and W.F.B. senior research assistant of this fund. J.V.P. receives a fellowship of the Belgian Instituut tot Aanmoediging van het Wetenschappelijk Onderzoek in Nijverheid en Landbouw.
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Van Parijs, J., Broekaert, W.F., Goldstein, I.J. et al. Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta 183, 258–264 (1991). https://doi.org/10.1007/BF00197797
- Hevea (antifungal protein)
- Plant-pathogen interaction
- Resistance (to fungi)