NDLI: An OTU deubiquitinating enzyme in Eimeria tenella interacts with Eimeria tenella virus RDRP

Content Provider	Springer Nature : BioMed Central
Author	Wang, Pu Li, Jianhua Gong, Pengtao Wang, Weirong Ai, Yongxing Zhang, Xichen
Abstract	Background Chicken coccidiosis, a disease caused by seven species of Eimeria (Apicomplexa: Coccidia), inflicts severe economic losses on the poultry industry. Eimeria tenella is the one of the most virulent species pathogenic to chickens. Many parasitic protozoans are parasitised by double-stranded (ds) RNA viruses, and the influence of protozoan viruses on parasitic protozoans has been extensively reported. E. tenella RNA virus 1 (Etv) was identified in E. tenella, and the complete genome sequence of Etv was analysed. Here, we screened Etv-RNA-dependent RNA polymerase (RDRP)-interacting host protein E. tenella ovarian tumour (OTU) protein-like cysteine protease (Et-OTU) using a yeast two-hybrid system with pGBKT7-RDRP plasmid serving as bait. A previous study demonstrated that Et-OTU could regulate the telomerase activity of E. tenella, indicating that Et-OTU affects E. tenella proliferation. However, whether Etv-RDRP affects the molecular biological characteristics of E. tenella by interacting with OTU remains unclear. Results We obtained seven positive clones from the initial screen, and six of the seven preys were identified as false-positives. Finally, we identified an RDRP-associated protein predicted to be an E. tenella OTU protein. A α-galactosidase assay showed that the bait vector did not activate the GAL4 reporter gene, indicating no autoactivation activity from the RDRP bait fusion. Pull-down and co-immunoprecipitation assays verified the interaction between Et-OTU and Etv-RDRP both intracellularly and extracellularly. Additionally, Et-OTU was able to deconjugate K48- and K6-linked di-ubiquitin (di-Ub) chains in vitro but not K63-, K11-, K29-, or K33-linked di-Ub chains. The C239A and H351A mutations eliminated the deubiquitinase (DUB) activity of Et-OTU, whereas the D236A mutation did not. Additionally, when combined with RDRP, the DUB activity of Et-OTU towards K48- and K6-linked chains was significantly enhanced. Conclusion Etv-RDRP interacts with Et-OTU both intracellularly and extracellularly. Etv-RDRP enhances the hydrolysis of Et-OTU to K6- or K48-linked ubiquitin chains. This study lays the foundation for further research on the relationship between E. tenella and Etv.
Related Links	https://parasitesandvectors.biomedcentral.com/counter/pdf/10.1186/s13071-018-2626-x.pdf
Ending Page	11
Page Count	11
Starting Page	1
File Format	HTM / HTML
ISSN	17563305
DOI	10.1186/s13071-018-2626-x
Journal	Parasites & Vectors
Issue Number	1
Volume Number	11
Language	English
Publisher	BioMed Central
Publisher Date	2018-01-31
Access Restriction	Open
Subject Keyword	Parasitology Entomology Tropical Medicine Infectious Diseases Veterinary Medicine Veterinary Science Virology Eimeria tenella Etv-RDRP Et-OTU Interaction Deubiquitinase Mutation Enhanced Veterinary Medicine/Veterinary Science
Content Type	Text
Resource Type	Article
Subject	Veterinary Infectious Diseases Parasitology
Journal Impact Factor	3/2023
5-Year Journal Impact Factor	3.3/2023

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