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First published online November 10, 2006; 10.1104/pp.106.087981

Plant Physiology 144:662-672 (2007)
© 2007 American Society of Plant Biologists

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A Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes1,[W],[OA]

Els J.M. Van Damme*, Raphaël Culerrier, Annick Barre, Richard Alvarez, Pierre Rougé and Willy J. Peumans

Department of Molecular Biotechnology, Laboratory of Biochemistry and Glycobiology, Ghent University, 9000 Gent, Belgium (E.J.M.V.D., W.J.P.); Surfaces Cellulaires et Signalisation chez les Végétaux, Unité Mixte de Recherche, Centre National de la Recherche Scientifique, Université Paul Sabatier 5546, Pôle de Biotechnologies Végétales, 31326 Castanet-Tolosan, France (R.C., A.B., P.R.); and Department of Biochemistry and Molecular Biology, University of Oklahoma, Health Sciences Center, Oklahoma City, Oklahoma 73104 (R.A.)

A lectin has been identified in black locust (Robinia pseudoacacia) bark that shares approximately 50% sequence identity with plant class V chitinases but is essentially devoid of chitinase activity. Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferentially binds to high-mannose N-glycans comprising the proximal pentasaccharide core structure. Closely related orthologs of RobpsCRA could be identified in the legumes Glycine max, Medicago truncatula, and Lotus japonicus but in no other plant species, suggesting that this novel lectin family most probably evolved in an ancient legume species or possibly an earlier ancestor. This identification of RobpsCRA not only illustrates neofunctionalization in plants, but also provides firm evidence that plants are capable of developing a sugar-binding domain from an existing structural scaffold with a different activity and accordingly sheds new light on the molecular evolution of plant lectins.


1 This work was supported by the Fund for Scientific Research-Flanders (project no. G.0201.04) and the Research Council of Ghent University. The glycan array analysis was conducted by the Protein-Glycan Interaction Core H of the Consortium for Functional Glycomics, funded by the National Institute of General Medical Sciences (grant no. GM62116).

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Els J.M. Van Damme (elsjm.vandamme{at}ugent.be).

[W] The online version of this article contains Web-only data.

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www.plantphysiol.org/cgi/doi/10.1104/pp.106.087981

* Corresponding author; e-mail elsjm.vandamme{at}ugent.be; fax 32–92646219.

Received August 4, 2006; accepted November 4, 2006; published November 10, 2006.




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