Open AccessAnalysis of the interactome of Schistosoma mansoni histone deacetylase 8
Author(s) -
Stéphanie Caby,
Lucile Pagliazzo,
Julien Lancelot,
JeanMichel Saliou,
Nicolas Bertheaume,
Raymond J. Pierce,
Emmanuel Roger
Publication year - 2017
Publication title -
plos neglected tropical diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.99
H-Index - 135
eISSN - 1935-2735
pISSN - 1935-2727
DOI - 10.1371/journal.pntd.0006089
Subject(s) - interactome , biology , histone deacetylase , immunoprecipitation , microbiology and biotechnology , schistosoma mansoni , stable isotope labeling by amino acids in cell culture , proteomics , histone , biochemistry , dna , schistosomiasis , zoology , gene , helminths
Background Histone deacetylase 8 from Schistosoma mansoni ( Sm HDAC8) is essential to parasite growth and development within the mammalian host and is under investigation as a target for the development of selective inhibitors as novel schistosomicidal drugs. Although some protein substrates and protein partners of human HDAC8 have been characterized, notably indicating a role in the function of the cohesin complex, nothing is known of the partners and biological function of Sm HDAC8. Methodology/Principal findings We therefore employed two strategies to characterize the Sm HDAC8 interactome. We first used Sm HDAC8 as a bait protein in yeast two-hybrid (Y2H) screening of an S . mansoni cDNA library. This allowed the identification of 49 different sequences encoding proteins. We next performed co-immunoprecipitation (Co-IP) experiments on parasite extracts with an anti- Sm HDAC8 antibody. Mass spectrometry (MS) analysis allowed the identification of 160 different proteins. Conclusions/Significance Sm HDAC8 partners are involved in about 40 different processes, included expected functions such as the cohesin complex, cytoskeleton organization, transcriptional and translational regulation, metabolism, DNA repair, the cell cycle, protein dephosphorylation, proteolysis, protein transport, but also some proteasome and ribosome components were detected. Our results show that Sm HDAC8 is a versatile deacetylase, potentially involved in both cytosolic and nuclear processes.