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Title: | Contribution of the carbohydrate-binding ability of Vatairea guianensis lectin to induce edematogenic activity |
Authors: | Marques, Gabriela Fernandes Oliveira Osterne, Vinicius José Silva Almeida, Livia M. Oliveira, Messias Vital Brizeno, Luiz André Cavalcante Pinto-Junior, Vanir Reis Santiago, Mayara Quiroz Neco, Antonio Hadson Bastos Mota, Mario Rogerio Lima Souza, Luis Augusto Gomes Nascimento, K. S. Pires, Alana de Freitas Cavada, B. S. Assreuy, Ana Maria Sampaio |
Keywords: | Carbohydrate Galactose Indometacin Interleukin-1beta N Acetylgalactosamine Ng-nitroarginine Methyl Ester Plant Lectin Prostaglandin Thalidomide Plant Lectin Chromatography, Affinity Animals Experiment Animals Model Antiinflammatory Activity Area Under The Curve Binding Site Bioinformatics Controlled Study Dose Response Drug Activity Drug Isolation Edematogenic Activity Fabaceae Immunohistochemistry In Vivo Study Ion Exchange Chromatography Metal Binding Minimum Inhibitory Concentration Molecular Docking Molecular Model Nonhuman Paw Edema Paw Tissue Seed Plant Protein Domain Protein Secondary Structure Rat Vatairea Guianensis Vatairea Macrocarpa Animals Chemically Induced Chemistry Edema Fabaceae Isolation And Purification Metabolism Molecular Docking Pathology Wistar Rat Animal Edema Fabaceae Molecular Docking Simulation Plant Lectins Rats Rats, Wistar |
Issue Date: | 2017 |
metadata.dc.publisher.journal: | Biochimie |
metadata.dc.relation.ispartof: | Volume 140, Pags. 58-65 |
Abstract: | Vatairea guianensis lectin (VGL), Dalbergiae tribe, is a N-acetyl-galactosamine (GalNAc)/Galactose (Gal) lectin previously purified and characterized. In this work, we report its structural features, obtained from bioinformatics tools, and its inflammatory effect, obtained from a rat paw edema model. The VGL model was obtained by homology with the lectin of Vatairea macrocarpa (VML) as template, and we used it to demonstrate the common characteristics of legume lectins, such as the jellyroll motif and presence of a metal-binding site in the vicinity of the carbohydrate-recognition domain (CRD). Protein-ligand docking revealed favorable interactions with N-acetyl-D-galactosamine, D-galactose and related sugars as well as several biologically relevant N- and O-glycans. In vivo testing of paw edema revealed that VGL induces edematogenic effect involving prostaglandins, interleukins and VGL CRD. Taken together, these data corroborate with previous reports showing that VGL interacts with N- and/or O-glycans of molecular targets, particularly in those presenting galactosides in their structure, contributing to the lectin inflammatory effect. © 2017 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM) |
metadata.dc.identifier.doi: | 10.1016/j.biochi.2017.06.008 |
Appears in Collections: | Artigos |
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