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Future Med Chem. 2015;7(6):765-82. doi: 10.4155/fmc.15.24.

Schistosome sirtuins as drug targets.

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Center for Infection & Immunity of Lille (CIIL), INSERM U1019 - CNRS UMR 8204, Université de Lille, Institut Pasteur de Lille, 1 rue Professeur Calmette, 59019 Lille Cedex, France.


The sirtuins form a superfamily of evolutionarily conserved NAD(+)-dependent protein N-ϵ-acyl-lysine (AcK) deacylases with roles in a variety of key cellular processes. Sirtuins have a broadly conserved overall structure with a catalytic site formed by a hydrophobic channel between the NAD(+)-binding Rossmann fold domain and a smaller Zn(2+)-binding domain. Schistosomes express five members of the sirtuin family and generic sirtuin inhibitors induce apoptosis and death in schistosome larvae, the disruption of adult worm pairs, inhibition of egg laying and damage to the male and female worm reproductive systems. Sirtuins in schistosomes and other parasitic flatworms present structural differences from their human orthologues that should allow the development of selective inhibitors that can be developed as drug leads.

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