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.
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November 2002
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Research Article|
November 01 2002
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
Corinne HOULÈS ASTOUL;
Corinne HOULÈS ASTOUL
∗Institut de Pharmacologie et Biologie Structurale, UMR-CNRS 5089, 205 Route de Narbonne, 31077 Toulouse Cedex 4, France
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Willy J. PEUMANS;
Willy J. PEUMANS
†Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem De Croylaan 42, 3001 Leuven, Belgium,
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Els J.M. van DAMME;
Els J.M. van DAMME
†Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Willem De Croylaan 42, 3001 Leuven, Belgium,
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Annick BARRE;
Annick BARRE
∗Institut de Pharmacologie et Biologie Structurale, UMR-CNRS 5089, 205 Route de Narbonne, 31077 Toulouse Cedex 4, France
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Yves BOURNE;
Yves BOURNE
‡Architecture et Fonction des Macromolécules Biologiques, UMR-CNRS 9039, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France
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Pierre ROUGÉ
Pierre ROUGÉ
1
∗Institut de Pharmacologie et Biologie Structurale, UMR-CNRS 5089, 205 Route de Narbonne, 31077 Toulouse Cedex 4, France
1To whom correspondence should be addressed (e-mail Pierre.Rouge@ipbs.fr).
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Publisher: Portland Press Ltd
Received:
May 31 2002
Revision Received:
July 17 2002
Accepted:
August 08 2002
Accepted Manuscript online:
August 09 2002
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2002
2002
Biochem J (2002) 367 (3): 817–824.
Article history
Received:
May 31 2002
Revision Received:
July 17 2002
Accepted:
August 08 2002
Accepted Manuscript online:
August 09 2002
Citation
Corinne HOULÈS ASTOUL, Willy J. PEUMANS, Els J.M. van DAMME, Annick BARRE, Yves BOURNE, Pierre ROUGÉ; 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. Biochem J 1 November 2002; 367 (3): 817–824. doi: https://doi.org/10.1042/bj20020856
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