Please use this identifier to cite or link to this item: https://repositorio.inpa.gov.br/handle/1/15718
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
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