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

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...

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Bibliographic Details
Published in:Biochimie 2017-09, Vol.140, p.58-65
Main Authors: Marques, Gabriela F.O., Osterne, Vinicius J.S., Almeida, Livia M., Oliveira, Messias V., Brizeno, Luiz A.C., Pinto-Junior, Vanir R., Santiago, Mayara Q., Neco, Antonio H.B., Mota, Mario R.L., Souza, Luiz A.G., Nascimento, Kyria S., Pires, Alana F., Cavada, Benildo S., Assreuy, Ana M.S.
Format: Article
Language:English
Subjects:
Animals
Edema - chemically induced
Edema - metabolism
Edema - pathology
Fabaceae - chemistry
Inflammation
Lectin
Molecular docking
Molecular Docking Simulation
Molecular modeling
Plant Lectins - chemistry
Plant Lectins - isolation & purification
Plant Lectins - toxicity
Rats
Rats, Wistar
Vatairea guianensis
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Summary: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. •The three-dimensional structure of VGL was predicted by molecular modeling.•The interactions of VGL with galactosides was determined.•Docking of VGL with representative N- and O-glycans was performed.•The inflammatory effect of VGL was determined in vivo.•The inflammatory effect of VGL involves prostaglandins, interleukins and VGL CRD.
ISSN:0300-9084
1638-6183
DOI:10.1016/j.biochi.2017.06.008