Ubiquitin-specific proteases are differentially expressed throughout the Schistosoma mansoni life cycle

Abstract

BackgroundThe ubiquitination process can be reversed by deubiquitinating enzymes (DUBs). These proteases are involved in ubiquitin processing, in the recovery of modified ubiquitin trapped in inactive forms, and in the recycling of ubiquitin monomers from polyubiquitinated chains. The diversity of DUB functions is illustrated by their number and variety of their catalytic domains with specific 3D architectures. DUBs can be divided into five subclasses: ubiquitin C-terminal hydrolases (UCHs), ubiquitin-specific proteases (USPs or UBPs), ovarian tumour proteases (OTUs), Machado-Joseph disease proteases (MJDs) and JAB1/MPN/Mov34 metalloenzymes (JAMMs).MethodsConsidering the role that the ubiquitin-proteasome system has been shown to play during the development of Schistosoma mansoni, our main goal was to identify and characterize SmUSPs. Here, we showed the identification of putative ubiquitin-specific proteases using bioinformatic approaches. We also evaluated the gene expression profile of representative USP family members using qRT-PCR.ResultsWe reported 17 USP family members in S. mansoni that present a conservation of UCH domains. Furthermore, the putative SmUSP transcripts analysed were detected in all investigated stages, showing distinct expression during S. mansoni development. The SmUSPs exhibiting high expression profiles were SmUSP7, SmUSP8, SmUSP9x and SmUSP24.ConclusionS. mansoni USPs showed changes in expression levels for different life cycle stages indicating their involvement in cellular processes required for S. mansoni development. These data will serve as a basis for future functional studies of USPs in this parasite.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-015-0957-4) contains supplementary material, which is available to authorized users.

Epigenetic and parasitological parameters are modulated in EBi3-/- mice infected with Schistosoma mansoni

“…Of the S. mansoni USPs analyzed here, SmUSP7 has the most domains, enabling the most functions, and this SmUSP therefore presents the highest level of expression independently of the strain [21]. USP7 orthologs have the ability to deubiquitinate histone acetyltransferase Tip60, which is involved in the acetylation of various histone H2A subtypes, deubiquitinate lysine 63 preventing the degradation of histone deacetylase Sirt7, and deubiquitinate histone H3 in a process involving the methylation of newly synthesized DNA by DNMT1 [34][35][36].…”

“…In the same approach the authors found that this protein has nuclear localization only and relates to oviposition [20]. Previous studies identified 17 USP orthologs in S. mansoni, by homology with 56 USPs present in H. sapiens, it was detected that the expression of these USPs is altered in stages of egg, cercariae, schistosomula and adult worms, reflecting a recycling of proteins used by the parasite during the evolutionary stage transition [21]. USPs can prevent different forms of degradation, i.e.…”

USP41 promotes breast cancer via regulating RACK1

“…The DUBs can be divided into 6 subclasses: ubiquitin C-terminal hydrolases (UCHs), ubiquitin-specific proteases (USPs or UBPs), ovarian tumor proteases (OTUs), Machado-Joseph disease proteases (MJDs), JAB1/MPN/Mov34 metalloenzymes (JAMMs), and monocyte chemotactic protein-induced deubiquitin family (MCPIPs). Among the 6 structurally different DUB families, the largest group comprises the ubiquitin-specific proteases (USPs) that belong to the cysteine protease family (10,11). Many studies have indicated that USPs regulate tumor formation by modulating the proliferation and death of cancer cells.…”

Clinicopathological and prognostic significance of ubiquitin‐specific peptidase 15 and its relationship with transforming growth factor‐β receptors in patients with pancreatic ductal adenocarcinoma

“…Dysfunctions of DUBs are associated with severe human diseases such as cancers and neurodegenerative disorders. Based on the features of the catalytic domain and functional similarities, DUBs are categorized into six subfamilies 10–12 . Among them, more than 50% of DUBs belong to the ubiquitin‐specific protease (USP) subfamily, many of which are correlated with lifespan control of oncogenes or the regulation of ubiquitin‐mediated signaling 13 …”