A nod factor binding lectin with apyrase activity from legume roots

A lectin isolated from the roots of the legume, Dolichos biflorus, binds to Nod factors produced by rhizobial strains that nodulate this plant and has a deduced amino acid sequence with no significant homology to any lectin r eported to date. This lectin also is an enzyme that catalyzes the hydrolysi s of phosphoanhydride bonds of nucleoside di- and triphosphates; the enzyme activity is increased in the presence of carbohydrate ligands, This lectin -nucleotide phosphohydrolase (LNP) has a substrate specificity characterist ic of the apyrase category of phosphohydrolases, and its sequence contains four motifs characteristic of this category of enzymes, LNP is present on t he surface of the root hairs, and treatment of roots with antiserum to LNP inhibits their ability to undergo root hair deformation and to form nodules on exposure to rhizobia. These properties suggest that this protein may pl ay a role in the rhizobium-legume symbiosis and/or in a related carbohydrat e recognition event endogenous to the plant.