Autores
Gabriela FO Marques, Vinicius JS Osterne, Livia M Almeida, Messias V Oliveira, Luiz AC Brizeno, Vanir R Pinto-Junior, Mayara Q Santiago, Antonio HB Neco, Mario RL Mota, Luiz AG Souza, Kyria S Nascimento, Alana F Pires, Benildo S Cavada, Ana MS Assreuy
Fecha de publicación
2017/9/1
Revista
Biochimie
Volumen
140
Páginas
58-65
Editor
Elsevier
Descripción
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 …
Artículos de Google Académico
GFO Marques, VJS Osterne, LM Almeida, MV Oliveira… - Biochimie, 2017