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Concanavalin A is a plant lectin that has been found in jack bean (C. ensiformis) and is involved in plant defense.1 It is formed from the 290-amino acid precursor protein pro-concanavalin A via deglycosylation by N-glycanase, peptide cleavage, and re-ligation to form the mature 237-amino acid monomer, which oligomerizes to form a tetramer. Each concanavalin A monomer has a carbohydrate recognition domain, which binds to α-D-mannose, α-D-glucose, and β-D-fructose, and a metal binding site that is involved in stability.1,2 Concanavalin A has diverse biological activities, including erythrocyte agglutination, mitogenic stimulation, and anticancer activity.1,2,3 It has been used in affinity purification of various glycoproteins, as well as to induce T cell activation in vitro and liver injury in experimental mouse models of autoimmune hepatitis.4,5,6
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1. Concanavalin -
2. Concanavalin A as a promising lectin-
3. Induction of apoptosis by concanavalin A and its molecular mechanisms in cancer cells. Autophagy 5(3), 432-433 (2009).
4. Concanavalin A-
5. The use of concanavalin A to study the immunoregulation of human T cells. Clin. Exp. Immunol. 46(2), 237-249 (1981).
6. Immune mechanisms of concanavalin A model of autoimmune hepatitis. World J. Gastroenterol. 18(2), 119-125 (2012).