ArticlePLoS neglected tropical diseases2011
Characterisation of the Trichinella spiralis deubiquitinating enzyme, TsUCH37, an evolutionarily conserved proteasome interaction partner.
Article in PLoS neglected tropical diseases, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- The emerging role of Deubiquitinases (DUBs) in parasites: A foresight review.Frontiers in cellular and infection microbiology · 2022Review
- Molecular Docking and In Silico Simulation ofBioMed research international · 2022Article
- Nedd8 hydrolysis by UCH proteases in Plasmodium parasites.PLoS pathogens · 2019Article
- Ubiquitin recognition of BAP1: understanding its enzymatic function.Bioscience reports · 2017Article
- Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights.The FEBS journal · 2017Review
- Ubiquitin-Dependent Modification of Skeletal Muscle by the Parasitic Nematode, Trichinella spiralis.PLoS pathogens · 2016Article
- Molecular characterization of a cathepsin F-like protease in Trichinella spiralis.Parasites & vectors · 2015Article
- Article
- Deubiquitinating enzymes as promising drug targets for infectious diseases.Current pharmaceutical design · 2013Review
- Detection of ubiquitin-proteasome enzymatic activities in cells: application of activity-based probes to inhibitor development.Biochimica et biophysica acta · 2012Review
- Ubiquitin-based probes prepared by total synthesis to profile the activity of deubiquitinating enzymes.Chembiochem : a European journal of chemical biology · 2012Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundTrichinella spiralis is a zoonotic parasitic nematode that causes trichinellosis, a disease that has been identified on all continents except Antarctica. During chronic infection, T. spiralis larvae infect skeletal myofibres, severely disrupting their differentiation state. METHODOLOGY AND
resultsAn activity-based probe, HA-Ub-VME, was used to identify deubiquitinating enzyme (DUB) activity in lysate of T. spiralis L1 larvae. Results were analysed by immuno-blot and immuno-precipitation, identifying a number of potential DUBs. Immuno-precipitated proteins were subjected to LC/MS/MS, yielding peptides with sequence homology to 5 conserved human DUBs: UCH-L5, UCH-L3, HAUSP, OTU 6B and Ataxin-3. The predicted gene encoding the putative UCH-L5 homologue, TsUCH37, was cloned and recombinant protein was expressed and purified. The deubiquitinating activity of this enzyme was verified by Ub-AMC assay. Co-precipitation of recombinant TsUCH37 showed that the protein associates with putative T. spiralis proteasome components, including the yeast Rpn13 homologue ADRM1. In addition, the UCH inhibitor LDN-57444 exhibited specific inhibition of recombinant TsUCH37 and reduced the viability of cultured L1 larvae.
conclusionsThis study reports the identification of the first T. spiralis DUB, a cysteine protease that is putatively orthologous to the human protein, hUCH-L5. Results suggest that the interaction of this protein with the proteasome has been conserved throughout evolution. We show potential for the use of inhibitor compounds to elucidate the role of UCH enzymes in T. spiralis infection and their investigation as therapeutic targets for trichinellosis.
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