Conservation and developmental expression of ubiquitin isopeptidases in Schistosoma mansoni

Memórias do Instituto Oswaldo Cruz

Roberta Verciano Pereira¹  Helaine Graziele Santos Vieira¹  Victor Fernandes De Oliveira¹  Matheus De Souza Gomes¹  Liana Konovaloff Jannotti Passos¹  William De Castro Borges¹  Renata Guerra-sá¹ 

关键词: deubiquitinating enzymes;    ubiquitin C-terminal hydrolase;    differential expression;    deubiquitination activity;   

DOI  :  10.1590/0074-0276130107

来源: SciELO

【 摘 要 】

Several genes related to the ubiquitin (Ub)-proteasome pathway, including those coding for proteasome subunits and conjugation enzymes, are differentially expressed during the Schistosoma mansoni life cycle. Although deubiquitinating enzymes have been reported to be negative regulators of protein ubiquitination and shown to play an important role in Ub-dependent processes, little is known about their role in S. mansoni . In this study, we analysed the Ub carboxyl-terminal hydrolase (UCHs) proteins found in the database of the parasite’s genome. An in silicoana- lysis (GeneDB and MEROPS) identified three different UCH family members in the genome, Sm UCH-L3, Sm UCH-L5 and SmBAP-1 and a phylogenetic analysis confirmed the evolutionary conservation of the proteins. We performed quantitative reverse transcription-polymerase chain reaction and observed a differential expression profile for all of the investigated transcripts between the cercariae and adult worm stages. These results were corroborated by low rates of Z-Arg-Leu-Arg-Gly-Gly-AMC hydrolysis in a crude extract obtained from cercariae in parallel with high Ub conjugate levels in the same extracts. We suggest that the accumulation of ubiquitinated proteins in the cercaria and early schistosomulum stages is related to a decrease in 26S proteasome activity. Taken together, our data suggest that UCH family members contribute to regulating the activity of the Ub-proteasome system during the life cycle of this parasite.

【 授权许可】

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