The size, shape and specificity of the sugar-binding site of the jacalin-related lectins is profoundly affected by the proteolytic cleavage of the subunits

Author:

ASTOUL Corinne HOULÈS1,PEUMANS Willy J.2,DAMME Els J.M. van2,BARRE Annick1,BOURNE Yves3,ROUGÉ Pierre1

Affiliation:

1. Institut de Pharmacologie et Biologie Structurale, UMR-CNRS 5089, 205 Route de Narbonne, 31077 Toulouse Cedex 4, France

2. Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem De Croylaan 42, 3001 Leuven, Belgium,

3. Architecture et Fonction des Macromolécules Biologiques, UMR-CNRS 9039, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France

Abstract

Mannose-specific lectins with high sequence similarity to jacalin and the Maclura pomifera agglutinin have been isolated from species belonging to the families Moraceae, Convolvulaceae, Brassicaceae, Asteraceae, Poaceae and Musaceae. Although these novel mannose-specific lectins are undoubtedly related to the galactose-specific Moraceae lectins there are several important differences. Apart from the obvious differences in specificity, the mannose- and galactose-specific jacalin-related lectins differ in what concerns their biosynthesis and processing, intracellular location and degree of oligomerization of the protomers. Taking into consideration that the mannose-specific lectins are widely distributed in higher plants, whereas their galactose-specific counterparts are confined to a subgroup of the Moraceae sp. one can reasonably assume that the galactose-specific Moraceae lectins are a small-side group of the main family. The major change that took place in the structure of the binding site of the diverging Moraceae lectins concerns a proteolytic cleavage close to the N-terminus of the protomer. To corroborate the impact of this change, the specificity of jacalin was re-investigated using surface plasmon resonance analysis. This approach revealed that in addition to galactose and N-acetylgalactosamine, the carbohydrate-binding specificity of jacalin extends to mannose, glucose, N-acetylmuramic acid and N-acetylneuraminic acid. Owing to this broad carbohydrate-binding specificity, jacalin is capable of recognizing complex glycans from plant pathogens or predators.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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