Concanavalin A is a unique lectin purified from the jack bean, C. ensiformis, that selectively cross-links cell-surface glycoproteins and affects the initiation of cell agglutination, mitogenesis, and apoptosis. Concanavalin A specifically binds to α-mannose and α-galactose structures found in sugars, glycoproteins, and glycolipids and has been used in affinity chromatography purifications of various glycoproteins and cellular structures. At 20 mg/kg concanavalin A is also used to induce liver injury in experimental mouse models of autoimmune hepatitis in order to study immune regulation by macrophages and T cells. Concanavalin A is toxic to several tumor cell lines and has been reported to induce programmed cell death of cortical neurons by a mechanism similar to that of the amyloid β peptide.
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A lectin mitogen that binds specifically to and agglutinates transforms into tumors. It binds to glucose
and mannose residues in the surface.
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Concanavalin A is a protein containing only β-sheets in its structure, and belongs to the legume lectins family.
