Pereira Roberta V, de S Gomes Matheus, Olmo Roenick P, Souza Daniel M, Cabral Fernanda J, Jannotti-Passos Liana K, Baba Elio H, Andreolli Andressa B P, Rodrigues Vanderlei, Castro-Borges William, Guerra-Sá Renata
Núcleo de Pesquisas em Ciências Biológicas, Universidade Federal de Ouro Preto, Morro do Cruzeiro, Ouro Preto, MG, Brasil.
Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, Patos de Minas, MG, Brasil.
Parasit Vectors. 2015 Jun 26;8:349. doi: 10.1186/s13071-015-0957-4.
The 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).
Considering 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.
We 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.
S. 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.
去泛素化酶（DUBs）可逆转泛素化过程。这些蛋白酶参与泛素加工、回收被困于无活性形式的修饰泛素以及从多聚泛素化链中回收泛素单体。DUB功能的多样性体现在其数量以及具有特定三维结构的催化结构域的种类上。DUBs可分为五个亚类：泛素C末端水解酶（UCHs）、泛素特异性蛋白酶（USPs或UBPs）、卵巢肿瘤蛋白酶（OTUs）、马查多-约瑟夫病蛋白酶（MJDs）和JAB1/MPN/Mov34金属酶（JAMMs）。
鉴于泛素-蛋白酶体系统在曼氏血吸虫发育过程中已显示出的作用，我们的主要目标是鉴定和表征曼氏血吸虫的SmUSPs。在此，我们展示了使用生物信息学方法鉴定推定的泛素特异性蛋白酶。我们还使用qRT-PCR评估了代表性USP家族成员的基因表达谱。
我们报道了曼氏血吸虫中有17个USP家族成员，它们具有UCH结构域的保守性。此外，在所分析的所有发育阶段均检测到了推定的SmUSP转录本，在曼氏血吸虫发育过程中呈现出不同的表达情况。表达水平较高的SmUSPs为SmUSP7、SmUSP8、SmUSP9x和SmUSP24。
曼氏血吸虫的USPs在不同生命周期阶段的表达水平发生变化，表明它们参与了曼氏血吸虫发育所需的细胞过程。这些数据将为该寄生虫中USPs的未来功能研究提供基础。
