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Plant Physiology Preview Published on May 1, 2008; 10.1104/pp.108.116764
OPEN ACCESS ARTICLE
Received January 25, 2008 THE OLD EUONYMUS EUROPAEUS AGGLUTININ REPRESENTS A NOVEL FAMILY OF UBIQUITOUS PLANT PROTEINS
Laboratory of Biochemistry and Glycobiology, Department of Molecular Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium; Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA; Rega institute, Laboratory of Molecular Immunology, Katholieke Universiteit Leuven, Minderbroedersstraat 10, 3000 Leuven, Belgium; Unit for Structural Biology, L-ProBE, Ghent University, K.L. Ledeganckstraat 35, 9000 Ghent, Belgium * Corresponding author; email: ElsJM.VanDamme{at}UGent.be.
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 post-translational processing apart from the removal of a 6-residue N-terminal peptide. Glycan array screening confirmed the previously reported high reactivity of EEA towards 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. BLAST 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 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.
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