Canavalia bonariensis lectin: Molecular bases of glycoconjugates interaction and antiglioma potential.

Autor:	Cavada BS; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil. Electronic address: bscavada@ufc.br., Silva MTL; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil., Osterne VJS; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil., Pinto-Junior VR; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil., Nascimento APM; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil., Wolin IAV; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil., Heinrich IA; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil., Nobre CAS; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil., Moreira CG; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil., Lossio CF; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil., Rocha CRC; Universidade Federal de Pernambuco (UFPE), Pernambuco, Recife, Brazil., Martins JL; Universidade Federal de Pelotas (UFPel), Pelotas, Rio Grande do Sul, Brazil., Nascimento KS; Universidade Federal do Ceará, Fortaleza, Ceará, Brazil., Leal RB; Universidade Federal de Santa Catarina (UFSC), Florianópolis, Santa Catarina, Brazil. Electronic address: rbleal@gmail.com.
Jazyk:	angličtina
Zdroj:	International journal of biological macromolecules [Int J Biol Macromol] 2018 Jan; Vol. 106, pp. 369-378. Date of Electronic Publication: 2017 Aug 10.
DOI:	10.1016/j.ijbiomac.2017.08.023
Abstrakt:	CaBo is a mannose/glucose-specific lectin purified from seeds of Canavalia bonariensis. In the present work, we report the CaBo crystal structure determined to atomic resolution in the presence of X-man, a specific ligand. Similar to the structural characteristics of other legume lectins, CaBo presented the jellyroll motif, a metal binding site occupied by calcium and manganese ions close to the carbohydrate-recognition domain (CRD). In vitro test of CaBo cytotoxicity against glioma cells demonstrated its ability to decrease the cellular viability and migration by induction of autophagy and cell death. Molecular docking simulations corroborate previous data indicating that the lectin's biological activities occur mostly through interactions with glycoproteins since the lectin interacted favorably with several N-glycans, especially those of the high-mannose type. Together, these results suggest that CaBo interacts with glycosylated cell targets and elicits a remarkable antiglioma activity. (Copyright © 2017 Elsevier B.V. All rights reserved.)
Databáze:	MEDLINE
Externí odkaz:	Full Text from ScienceDirect