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Publication Abstract from PubMed

Plant lectins, especially those purified from species of the Leguminosae family, represent the best-studied group of carbohydrate-binding proteins. Lectins purified from seeds of the Diocleinae subtribe exhibit a high degree of sequence identity notwithstanding that they show very distinct biological activities. Two main factors have been related to this feature: variance in key residues influencing the carbohydrate-binding site geometry and differences in the pH-dependent oligomeric state profile. In this work, we have isolated a lectin from Canavalia boliviana (Cbol) and solved its x-ray crystal structure in the unbound form and in complex with the carbohydrates Man(alpha1-3)Man(alpha1-O)Me, Man(alpha1-4)Man(alpha1-O)Me and 5-bromo-4-chloro-3-indolyl-alpha-D-mannose. We evaluated its oligomerization profile at different pH values using Small Angle X-ray Scattering and compared it to that of Concanavalin A. Based on predicted pKa-shifts of amino acids in the subunit interfaces we devised a model for the dimer-tetramer equilibrium phenomena of these proteins. Additionally, we demonstrated Cbol anti-inflammatory properties and further characterized them using in vivo and in vitro models.

Structural Studies of an Anti-Inflammatory Lectin from Canavalia boliviana Seeds in Complex with Dimannosides.,Bezerra GA, Viertlmayr R, Moura TR, Delatorre P, Rocha BA, do Nascimento KS, Figueiredo JG, Bezerra IG, Teixeira CS, Simoes RC, Nagano CS, de Alencar NM, Gruber K, Cavada BS PLoS One. 2014 May 27;9(5):e97015. doi: 10.1371/journal.pone.0097015. eCollection, 2014. PMID:24865454^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.