Contribution of the carbohydrate-binding ability of Vatairea guianensis lectin to induce edematogenic activity

• Autor(es): 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
• Data: 2020
• Origem: Oasisbr
• Assunto(s): 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
• Tipo de Documento: Artigo científico
• Idioma: Inglês

Descrição

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)