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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

The "Old" Euonymus europaeus Agglutinin Represents a Novel Family of Ubiquitous Plant Proteins^1,[W],[OA]

Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology (E.F., W.J.P., E.J.M.V.D.), and Unit for Structural Biology, Laboratory for Protein Biochemistry and Biomolecular Engineering (S.N.S.), Ghent University, 9000 Ghent, Belgium; Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322 (D.F.S.); and Rega Institute, Laboratory of Molecular Immunology, Katholieke Universiteit Leuven, 3000 Leuven, Belgium (P.P.)

Molecular cloning of the "old" but still unclassified Euonymus europaeus agglutinin (EEA) demonstrated that the lectin is a homodimeric protein composed of 152 residue subunits. Analysis of the deduced sequence indicated that EEA is synthesized without a signal peptide and undergoes no posttranslational processing apart from the removal of a six-residue N-terminal peptide. Glycan array screening confirmed the previously reported high reactivity of EEA toward blood group B oligosaccharides but also revealed binding to high mannose N-glycans, providing firm evidence for the occurrence of a plant carbohydrate-binding domain that can interact with structurally different glycans. Basic Local Alignment Search Tool searches indicated that EEA shares no detectable sequence similarity with any other lectin but is closely related evolutionarily to a domain that was first identified in some abscisic acid- and salt stress-responsive rice (Oryza sativa) proteins, and, according to the available sequence data, might be ubiquitous in Spermatophyta. Hence, EEA can be considered the prototype of a novel family of presumably cytoplasmic/nuclear proteins that are apparently ubiquitous in plants. Taking into account that some of these proteins are definitely stress related, the present identification of the EEA lectin domain might be a first step in the recognition of the involvement and importance of protein-glycoconjugate interactions in some essential cellular processes in Embryophyta.

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.108.116764

^* Corresponding author; e-mail elsjm.vandamme{at}ugent.be.

Received January 25, 2008; accepted April 25, 2008; published May 1, 2008.

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