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BioMed Research International
Volume 2013, Article ID 154542, 7 pages
Research Article

Toxicity and Binding Profile of Lectins from the Genus Canavalia on Brine Shrimp

1Integrated Laboratory of Biomolecules (LIBS-BioMol Group), Department of Pathology and Legal Medicine, Federal University of Ceará, 62042-280 Fortaleza, CE, Brazil
2Laboratory of Biologically Actives Molecules, Department of Biochemistry and Molecular Biology, Federal University of Ceará, 60440-970 Fortaleza, CE, Brazil
3Marine Biochemistry Laboratory, Fishing Engineering Department, Federal University of Ceará, 60440-970 Fortaleza, CE, Brazil

Received 16 July 2013; Accepted 24 October 2013

Academic Editor: Daiana Avila

Copyright © 2013 Francisco Vassiliepe Sousa Arruda et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.