Abstract
Lectins are sugar-binding proteins widely distributed in nature with many biological functions. Although many lectins have a remarkable biotechnological potential, some of them can be cytotoxic. Thus, the aim of this study was to assess the toxicity of five lectins, purified from seeds of different species of Canavalia genus. In order to determine the toxicity, assays with Artemia nauplii were performed. In addition, a fluorescence assay was carried out to evaluate the binding of lectins to Artemia nauplii. In order to verify the relationship between the structure of lectins and their cytotoxic effect, structural analysis was carried out to evaluate the volume of the carbohydrate recognition domain (CRD) of each lectin. The results showed that all lectins exhibited different toxicities and bound to a similar area in the digestive tract of Artemia nauplii. Concerning the structural analysis, differences in spatial arrangement and volume of CRD may explain the variation of the toxicity exhibited by each lectin. To this date, this is the first study that establishes a link between toxicity and structure of CRD from Diocleinae lectins.
Highlights
Lectins are sugar-binding proteins widely distributed in nature in organisms such as viruses, bacteria, fungi, plants, and animals [1]
Diocleinae lectins share the same carbohydrate recognition specificity for D-mannose and Dglucose, require divalent ions such as Ca2+ and Mn2+ to be biologically active, and contain a hydrophobic cavity that binds to phytohormones and other hydrophobic ligands
Canavalia lectins exhibited a range of different toxicities toward Artemia nauplii
Summary
Lectins are sugar-binding proteins widely distributed in nature in organisms such as viruses, bacteria, fungi, plants, and animals [1]. Some of these proteins bind mono- and oligosaccharides and reversibly but are devoid of catalytic activity and, in contrast to antibodies, are not products of an immune response [2]. Diocleinae lectins share the same carbohydrate recognition specificity for D-mannose and Dglucose, require divalent ions such as Ca2+ and Mn2+ to be biologically active, and contain a hydrophobic cavity that binds to phytohormones and other hydrophobic ligands. These ConA-like lectins induce different responses in biological assays; for example, when tested for stimulation of human lymphocyte proliferation in vitro, ConBr had a higher proliferation index than ConA, possibly due to minor changes in binding specificities [6]
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