Contribution of the carbohydrate-binding ability of Vatairea guianensis lectin to induce edematogenic activity
| Autor: | Mayara Queiroz Santiago, Alana de Freitas Pires, Vinicius Jose Da Silva Osterne, Luiz André Cavalcante Brizeno, Messias Vital Oliveira, Gabriela Fernandes Oliveira Marques, Ana Maria Sampaio Assreuy, Antonio Hadson Bastos Neco, Benildo Sousa Cavada, Luiz Augusto Gomes de Souza, Vanir Reis Pinto-Junior, Lívia Mendes de Almeida, Kyria S. Nascimento, Mário Rogério Lima Mota |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Molecular model Prostaglandin Interleukin-1beta Biochemistry Chromatography Affinity chemistry.chemical_compound 0302 clinical medicine Galactosides Dose Response Paw Edema Pathology Antiinflammatory Activity Edema Drug Isolation Protein Secondary Structure Area Under The Curve Edematogenic Activity In Vivo Study Isolation And Purification Plant Lectin Fabaceae General Medicine Wistar Rat N Acetylgalactosamine Immunohistochemistry Thalidomide Molecular Docking Molecular Docking Simulation Chemistry 030220 oncology & carcinogenesis Minimum Inhibitory Concentration medicine.symptom Plant Lectins Animals Experiment Ng-nitroarginine Methyl Ester Seed Plant Carbohydrate Glycosylation Bioinformatics Protein Domain Animals Model Drug Activity Inflammation Biology Chemically Induced Paw Tissue 03 medical and health sciences Vatairea Guianensis Vatairea Macrocarpa medicine Animals Controlled Study Ion Exchange Chromatography Rats Wistar Indometacin Animal Binding Site Lectin Galactose Molecular Model Nonhuman Rats 030104 developmental biology Metabolism chemistry Docking (molecular) biology.protein Rat Metal Binding |
| Zdroj: | Repositório Institucional do INPA Instituto Nacional de Pesquisas da Amazônia (INPA) instacron:INPA |
| Popis: | 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) |
| Databáze: | OpenAIRE |
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