Characterisation of the Trichinella spiralis Deubiquitinating Enzyme, TsUCH37, an Evolutionarily Conserved Proteasome Interaction Partner

• Published in: PLoS Neglected Tropical Diseases
• Main Authors: White, Rhiannon R., Miyata, Sachiko, Papa, Eliseo, Spooner, Eric, Gounaris, Kleoniki, Selkirk, Murray E., Artavanis-Tsakonas, Katerina
• Format: Text
• Language: English
• Published: Public Library of Science 2011
• Subjects: Research Article; Antarc*; Antarctica
• Online Access: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3186758; http://www.ncbi.nlm.nih.gov/pubmed/22013496; https://doi.org/10.1371/journal.pntd.0001340

Trichinella spiralis is a parasitic nematode that infects mammals indiscriminately. Although the biggest impact of trichinellosis is observed in developing countries, the parasite is found on all continents except Antarctica. In humans, Trichinella infection contributes globally to helminth related morbidity and disability adjusted life years. In animals, infection is implicated as a serious agricultural problem and drug treatment is largely ineffective. During chronic infection, larvae invade skeletal muscle cells, forming a nurse cell complex in which they become encysted. The nurse cell is a product of the severe disruption of the host cell homeostasis. Proteins of the Ub/proteasome pathway are highly conserved throughout evolution, and considering their importance in the regulation of cell homeostasis, provide interesting and novel therapeutic targets for various diseases. In order to target this system in parasites, pathogen proteins that play a role in this pathway must be identified. We report the identification of the first T. spiralis deubiquitinating enzyme, and show evidence that the function of this protein as a proteasome interaction partner has been evolutionarily conserved. We show that members of this enzyme family are important for T. spiralis survival and that the use of inhibitor compounds may help elucidate their role in infection.