Identification of high-affinity binding sites for the hepta-β-glucoside elicitor in membranes of the model legumes Medicago truncatula and Lotus japonicus

Previous studies have led to the identification and characterization of specific, high-affinity binding sites for a hepta-beta-glucoside elicitor in soybean. A survey of plant species for elicitor-binding activity reveals that among the plants tested, the hepta-beta-glucoside elicitor is only recognized by plants belonging to the legume family. We have characterized in detail the glucan elicitor-binding site in the model legume Medicago truncatula Gaertn., and partially characterized the site in torus japonicus. These sites have characteristics that ale very similar to the one in soybean, with dissociation constants of 4.7 and 8.9 nM respectively. The elicitor-binding sites from both plants are stable during solubilization with non-ionic alkylglycoside detergents. However. differences are observed in the abundance of the binding sites and their selectivity towards structurally related analogues of the hepta-beta-glucoside elicitor. Our results suggest that similar, but perhaps not identical. binding sites for the hepta-beta-glucoside elicitor exist, in diverse legumes, but not in plants outside of the legume family.