Exploring the carbohydrate-binding ability ofCanavalia bonariensislectin
in inflammation models
JOURNAL OF MOLECULAR RECOGNITION, (2020)DOI: 10.1002/jmr.2870, Early Access Date = JUL 2020
Abstract
Lectins are a group of proteins of non-immune origin recognized for
their ability to bind reversibly to carbohydrates. Researchers have been
intrigued by oligosaccharides and glycoconjugates for their involvement
as mediators of complex cellular events and then many biotechnological
applications of lectins are based on glycocode decoding and their
activities. Here, we report a structural and biological study of a
ConA-like mannose/glucose-specific lectin fromCanavalia
bonariensisseeds, CaBo. More specifically, we evaluate the binding of
CaBo with alpha-methyl-D-mannoside (MMA) and mannose-1,3-alpha-D-mannose
(M13) and the resultantin vivoeffects on a rat model of acute
inflammation. A virtual screening was also carried out to cover a larger
number of possible bindings of CaBo.In silicoanalysis demonstrated the
stability of CaBo interaction with mannose-type ligands, and the lectin
was able to induce acute inflammation in rats with the participation of
the carbohydrate recognition domain (CRD) and histamine release. These
results confirm the ability of CaBo to interact with hybrid and
high-mannoseN-glycans, supporting the hypothesis that CaBo's biological
activity occurs primarily through its interaction with cell surface
glycosylated receptors.