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

Abstract

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.

Inhibitory effect of Lonchocarpus araripensis lectin in rat acute models of inflammation

“…In addition to the documented role of endogenous mammalian lectins, exogenous lectins also exhibit immunomodulatory function (Rabinovich and Croci 2012). It has been shown that plant lectins possess anti-or pro-inflammatory effect in several murine models, being theses effects dependent on the administration route or the lectin binding sugar (Assreuy et al 1997, 2009, Marques et al 2017, Napimoga et al 2007. In general, lectins isolated from the genus Lonchocarpus show anti-inflammatory pattern either in mice or rat models of acute inflammation (Assreuy et al 1999, Alencar et al 2005, Napimoga et al 2007, except for LAL, being previously demonstrated only in mice (Pires et al 2016).…”

“…In respect to plant lectins isolated from the Dalbergieae tribe, those possessing binding affinity for galactose present local inflammatory effect, such as the lectins of Vatairea macrocarpa (Alencar et al 2003(Alencar et al , 2004(Alencar et al , 2007 and Vatairea guianensis (Marques et al 2017). On the other hand, those possessing binding affinity for N-acetylglucosamine present systemic anti-inflammatory effect, such as the lectins of Lonchocarpus sericeus (Alencar et al 2005, Napimoga et al 2007 and Lonchocarpus araripensis (Pires et al 2016).…”

ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships

“…These lectins can inhibit tumorigenesis by binding to glycosylated proteins on the membrane of cancer cells. It is well known that glycoconjugates play important roles in many biological processes, including cancer, with malignant cells usually presenting altered glycosylation patterns [11]. These changes in glycans allow preferential binding of lectin on cancer cells to induce the above effects.…”

“…These proteins are known to possess inflammatory, nociceptive, vasoactive, antiproliferative, antimicrobial, immunomodulatory, and antidepressant activities, among others [8,10]. Most of these biological activities are directly related to the ability of these proteins to interact with carbohydrates via the carbohydrate recognition domain (CRD) [11]. This interaction can be influenced by CRD conformation, which is defined by the amino acid composition, as well as the oligomerization state of these molecules, which may be dependent on the pH of the medium [12].…”

Differential vasodilator effect of Dioclea rostrata lectin in conductance and resistance arteries: Mechanisms and glycoconjugate binding relationships

“…Formation of GalNAcβ 1‐4GlcNAc can also occur in some complex glycans 36 . DRL interacted favourably with COMP1 with a score of −50.94, but not with COMP2, which can be explained by the presence of a sialic acid in its structure, as seen in other plant lectins 35,37 …”