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1.D.12 The Beauvericin (Beauvericin) Family

Beauvericin is a cyclic hexadepsipeptide consisting of an alternating sequence of 3 D-α hydroxy-iso-valeryl and 3 N-methylphenylalanyl residues. It was originally isolated from Beauveria bassiana but has been detected in various fungal species including Fusarium spp.  Beauvericin has antibiotic, insecticidal, apoptotic and cholesterol acyltransferase inhibiting activities.

Beauvericin is a cation-selective ionophore, transporting Na+, K+ and Ca2+. Activity has been demonstrated in liposomes and in myocytes and is blocked by La3+. Beauvericin (BEA) is a mycotoxin produced by many species of fungus Fusarium. BEA is a natural contaminant of cereals and cereals based products and possesses a wide variety of biological properties (Mallebrera et al. 2018). The mechanism of action is due to its ionophoric activity, that increases ion permeability in biological membranes. As a consequence, BEA causes cytotoxicity in several cell lines and can produce oxidative stress. Moreover, BEA is genotoxic (produces DNA fragmentation, chromosomal aberrations and micronucleus) and causes apoptosis with the involvement of the mitochondrial pathway. However, several antioxidant mechanisms protect cells against oxidative stress produced by BEA (Mallebrera et al. 2018). 

The reaction catalyzed by beauvericin is:

cation (in) cation (out)


References associated with 1.D.12 family:

Kouri, K., M. Lemmens, and R. Lemmens-Gruber. (2003). Beauvericin-induced channels in ventricular myocytes and liposomes. Biochim. Biophys. Acta 1609: 203-210. 12543382
Mallebrera, B., A. Prosperini, G. Font, and M.J. Ruiz. (2018). In vitro mechanisms of Beauvericin toxicity: A review. Food Chem Toxicol 111: 537-545. 29154952