Exploring the carbohydrate-binding ability of Canavalia bonariensis lectin in inflammation models.

Autor: Cavada BS; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil., Silva MTL; Departamento de Bioquímica, Universidade Federal de Santa Catarina, Florianópolis, Brazil., Osterne VJS; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil., Pinto-Junior VR; Departamento de Física, Universidade Federal do Ceará, Fortaleza, Brazil., Lossio CF; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil., Madeira JC; Instituto Superior de Ciências Biomédicas, Universidade Estadual do Ceará, Fortaleza, Brazil., Pereira MG; Instituto Superior de Ciências Biomédicas, Universidade Estadual do Ceará, Fortaleza, Brazil., Leal RB; Departamento de Bioquímica, Universidade Federal de Santa Catarina, Florianópolis, Brazil., Ferreira WP; Departamento de Física, Universidade Federal do Ceará, Fortaleza, Brazil., Nascimento KS; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil., Assreuy AMS; Instituto Superior de Ciências Biomédicas, Universidade Estadual do Ceará, Fortaleza, Brazil.
Jazyk: angličtina
Zdroj: Journal of molecular recognition : JMR [J Mol Recognit] 2020 Nov; Vol. 33 (11), pp. e2870. Date of Electronic Publication: 2020 Jul 09.
DOI: 10.1002/jmr.2870
Abstrakt: Lectins are a group of proteins of non-immune origin recognized for their ability to bind reversibly to carbohydrates. Researchers have been intrigued by oligosaccharides and glycoconjugates for their involvement as mediators of complex cellular events and then many biotechnological applications of lectins are based on glycocode decoding and their activities. Here, we report a structural and biological study of a ConA-like mannose/glucose-specific lectin from Canavalia bonariensis seeds, CaBo. More specifically, we evaluate the binding of CaBo with α-methyl-D-mannoside (MMA) and mannose-1,3-α-D-mannose (M13) and the resultant in vivo effects on a rat model of acute inflammation. A virtual screening was also carried out to cover a larger number of possible bindings of CaBo. In silico analysis demonstrated the stability of CaBo interaction with mannose-type ligands, and the lectin was able to induce acute inflammation in rats with the participation of the carbohydrate recognition domain (CRD) and histamine release. These results confirm the ability of CaBo to interact with hybrid and high-mannose N-glycans, supporting the hypothesis that CaBo's biological activity occurs primarily through its interaction with cell surface glycosylated receptors.
(© 2020 John Wiley & Sons Ltd.)
Databáze: MEDLINE
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