Open AccessNicotinamide inhibits Plasmodium falciparum Sir2 activity in vitro and parasite growth
Author(s) -
Prusty Dhaneswar,
Mehra Parul,
Srivastava Sandeep,
Shivange Amol V.,
Gupta Ashish,
Roy Nilanjan,
Dhar Suman Kumar
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2008.01135.x
Subject(s) - plasmodium falciparum , sirtuin , sirt2 , histone deacetylase , nicotinamide , biology , in vitro , sirtuin 1 , biochemistry , enzyme , histone , nad+ kinase , malaria , downregulation and upregulation , gene , immunology
Plasmodium falciparum sirtuin, PfSir2, contains histone deacetylase (HDAC) activity that may be central to the regulation of virulence gene expression in the parasites. Although a few reports have been published recently regarding in vitro and in vivo function of PfSir2, expression of the endogenous protein ( c . 30 kDa) has not been shown yet. Here we report the presence of PfSir2 in the parasite at the protein level by specific antibodies. HDAC activity of PfSir2 can be inhibited by nicotinamide, a product of sirtuin reaction. Surprisingly, we find that nicotinamide also delays parasite growth significantly in culture. These findings further our knowledge on PfSir2 and raise the possibility of using an inexpensive agent like nicotinamide as an antimalarial in combination with other antiparasitic drugs.