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Specific binding of a hypersensitive lignification elicitor from Puccinia graminis f.sp. tritici to the plasma membrane from wheat (Triticum aestivum L.)

Kogel, G., Beissmann, B., Reisener, H.J., Kogel, K.
Planta 1991 v.183 no.2 pp. 164-169
Triticum aestivum, Hordeum vulgare, Puccinia graminis, host-parasite relationships, disease resistance, lignification, glycoproteins, binding proteins, molecular weight, enzyme activity, rust diseases, leaves, immunocytochemistry, plasma membrane, binding sites
We have recently reported the isolation and characterization of a glycoprotein (Mr 67 000) from germ-tube walls of Puccinia graminis f. sp. tritici which elicits the cellular hypersensitive lignification response in wheat (G. Kogel et al., 1988, Physiol. Mol. Plant Pathol. 33, 173-185). The present study uses this glycoprotein, referred to as Pgt elicitor, to identify putative elicitor targets in wheat cell membranes. In enzyme-linked immunosorbent assays using anti-Pgt elicitor antibodies, specific binding sites for Pgt elicitor were detected in highly purified plasma-membrane vesicles of wheat (Triticum aestivum L.) primary leaf cells. Binding proved to be independent of the presence or absence in wheat of the Sr5 gene for rust resistance, and also occurred on barley (Hordeum vulgare L.) plasma membrane. The binding sites have an Mr of 30 000 and 33 000, respectively, and binding activity was not lost in the presence of sodium dodecyl sulfate. [14C]imido-Pgt elicitor was used to determine the apparent Kd value for specific binding, found to be 2.0 micromolar, and the maximum content of binding sites, found to be 250 pmol per mg of plasma-membrane protein. The relevance of the elicitor binding for the outcome of the interaction of P. graminis and wheat is discussed.