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dc.contributor.authorMarques, Gabriela Fernandes Oliveira-
dc.contributor.authorOsterne, Vinicius José Silva-
dc.contributor.authorAlmeida, Livia M.-
dc.contributor.authorOliveira, Messias Vital-
dc.contributor.authorBrizeno, Luiz André Cavalcante-
dc.contributor.authorPinto-Junior, Vanir Reis-
dc.contributor.authorSantiago, Mayara Quiroz-
dc.contributor.authorNeco, Antonio Hadson Bastos-
dc.contributor.authorMota, Mario Rogerio Lima-
dc.contributor.authorSouza, Luis Augusto Gomes-
dc.contributor.authorNascimento, K. S.-
dc.contributor.authorPires, Alana de Freitas-
dc.contributor.authorCavada, B. S.-
dc.contributor.authorAssreuy, Ana Maria Sampaio-
dc.date.accessioned2020-05-18T15:08:11Z-
dc.date.available2020-05-18T15:08:11Z-
dc.date.issued2017-
dc.identifier.urihttps://repositorio.inpa.gov.br/handle/1/15718-
dc.description.abstractVatairea 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)en
dc.language.isoenpt_BR
dc.relation.ispartofVolume 140, Pags. 58-65pt_BR
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Brazil*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/br/*
dc.subjectCarbohydrateen
dc.subjectGalactoseen
dc.subjectIndometacinen
dc.subjectInterleukin-1betaen
dc.subjectN Acetylgalactosamineen
dc.subjectNg-nitroarginine Methyl Esteren
dc.subjectPlant Lectinen
dc.subjectProstaglandinen
dc.subjectThalidomideen
dc.subjectPlant Lectinen
dc.subjectChromatography, Affinityen
dc.subjectAnimals Experimenten
dc.subjectAnimals Modelen
dc.subjectAntiinflammatory Activityen
dc.subjectArea Under The Curveen
dc.subjectBinding Siteen
dc.subjectBioinformaticsen
dc.subjectControlled Studyen
dc.subjectDose Responseen
dc.subjectDrug Activityen
dc.subjectDrug Isolationen
dc.subjectEdematogenic Activityen
dc.subjectFabaceaeen
dc.subjectImmunohistochemistryen
dc.subjectIn Vivo Studyen
dc.subjectIon Exchange Chromatographyen
dc.subjectMetal Bindingen
dc.subjectMinimum Inhibitory Concentrationen
dc.subjectMolecular Dockingen
dc.subjectMolecular Modelen
dc.subjectNonhumanen
dc.subjectPaw Edemaen
dc.subjectPaw Tissueen
dc.subjectSeed Planten
dc.subjectProtein Domainen
dc.subjectProtein Secondary Structureen
dc.subjectRaten
dc.subjectVatairea Guianensisen
dc.subjectVatairea Macrocarpaen
dc.subjectAnimalsen
dc.subjectChemically Induceden
dc.subjectChemistryen
dc.subjectEdemaen
dc.subjectFabaceaeen
dc.subjectIsolation And Purificationen
dc.subjectMetabolismen
dc.subjectMolecular Dockingen
dc.subjectPathologyen
dc.subjectWistar Raten
dc.subjectAnimalen
dc.subjectEdemaen
dc.subjectFabaceaeen
dc.subjectMolecular Docking Simulationen
dc.subjectPlant Lectinsen
dc.subjectRatsen
dc.subjectRats, Wistaren
dc.titleContribution of the carbohydrate-binding ability of Vatairea guianensis lectin to induce edematogenic activityen
dc.typeArtigopt_BR
dc.identifier.doi10.1016/j.biochi.2017.06.008-
dc.publisher.journalBiochimiept_BR
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