ConBr, the Lectin from Canavalia brasiliensis Mart. Seeds: Forty Years of Research

Abstract

Lectins are defined as proteins or glycoproteins capable of specific and reversible binding to carbohydrates. Inside this group of proteins, the most well-studied lectins belong to the Leguminosae family, and inside this family, the Diocleinae subtribe includes the most characterized lectin Concanavalin A (ConA), as well as ConBr, the lectin from Canavalia brasiliensis, the subject of this review. Since 1979, several studies have been published in the literature regarding this lectin, from its isolation and characterization to its several biological activities. This year, 2019, will mark 40 years since researchers have begun to study ConBr and 100 years since the discovery of ConA, making 2019 a momentous year for lectinology. Owing to the abundance of studies involving ConBr, this review will focus on ConBr’s purification, physicochemical properties, functional and structural analyses, biological activities and biotechnological applications. This will give researchers a broad glimpse into the potential of this lectin, as well as it characteristics, as we look ahead to its expanding applications in glycomics and biotechnology.

Purification and characterization of a highly thermostable GlcNAc-binding lectin from Collaea speciosa seeds

“…After addition of Ca 2+ or Mn 2+ ions, a partial restoration of the activity was observed, while full activity was recovered only after the addition of both divalent cations. These results show that CsL, similar to most Diocleinae lectins, is dependent on metal ions, such as Ca 2+ and Mn 2+ (Figure 3CD and Table 3) [7,51]. Judging from the absence of PAS staining CsL, does not have any covalently attached glycan in its structure in contrast to the positive control lectin (VML) (Figure 4) [52,53].…”

ConBr lectin modulates MAPKs and Akt pathways and triggers autophagic glioma cell death by a mechanism dependent upon caspase-8 activation

“…ConBr and ConA display high similarity of amino acid sequence and crystal structure. However, differences of biological activities have been well documented for these lectins [33,34]. Moreover, other lectins of the genre Canavalia, such as CaBo and ConV, showed similar effect only after 24 h treatment and at higher concentration (50-100 μg/mL) [28,29].…”

“…It is a glucose/mannose-specific lectin largely homologous to ConA, differing by only three residues [31,32]. Numerous studies have shown various biological actions of ConBr on different targets, including immune and nervous system cells [33][34][35].…”

Bioactivity of Chitosan-Based Particles Loaded with Plant-Derived Extracts for Biomedical Applications: Emphasis on Antimicrobial Fiber-Based Systems

“…They may form ion channels in the microbial membrane or inhibit adhesion of microbial proteins to host polysaccharide receptors. Hence, they are capable of precipitating polysaccharides and glycoproteins or agglutinating cells [82][83][84][85]. Overall, these changes are mostly induced by hydrophobic effects, covalent binding and hydrogen binding of their phenolic compounds [69].…”

“…Regardless, these proteins or glycoproteins are often positively charged, with disulphide bonds. Concanavalin A and galectin-1 are well-known examples, having as ligands Manα1-OCH 3 and Gal(β1→4)Glc, respectively [82][83][84][85]90].…”