Eimeria tenella
Ontology highlight
ABSTRACT:
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| Other | ||||
| etenella_all_ETH2_tags.gff.gz | Other | |||
| DRR003393.fastq.gz | Fastqsanger.gz | |||
| DRR033163.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 203 |
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Project description:Causes coccidiosis in domestic fowl
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Project description:Apicomplexa parasite Eimeria is the causative agent of coccidiosis, which leads to enteritis in animals and causes huge economic burden to the farm industry. The Apicomplexan Apetala2/ERF (ApiAP2) transcription factors have proved to play key roles in various processes in other Apicomplexa parasites. However, little is known about the function of ApiAP2s in Eimeria species. In this study, we functionally characterized an ApiAP2 by direct knockout mediated by CRISPR-Cas9. Our results showed that the invasion efficiency, total oocyst output and virulence to the host were significantly impaired after EtAP2-S1 depletion. RNA-Seq and CUT&Tag analyze showed that EtAP2-S1 targets on the promoters of numerous genes and its knockout results in upregulation of 59 sag genes. Additionally, the knockout strain exhibits significantly reduced virulence but provides excellent immune protection, which makes it a good vaccine candidate. This study demonstrates that EtAP2-S1 is a fitness coffering gene that suppress the expression of sag genes in E. tenella, and this is the first practice in developing gene knockout vaccine for the control of coccidiosis.
2024-12-01 | GSE282226 | GEO
Project description:Eimeria tenella is a high pathogenic coccidian that causes avain coccidiosis. Both Nitromezuril(NZL) and Ethanamizuril(EZL) are novel triazine compounds with high anticoccidial activity, but the mechanisms of their action are still unclear. This study explored the response of E.tenella to NZL and EZL by the study of changes in protein composition of the second-generation merozoites using label free quantification proteomics.After drug treatment, the merozoites were analyzed by LC-MS/MS. The identified proteins were annotated and analyzed by Gene ontology, Kyoto Encyclopedia of Genes and Genomes pathway and Protein-protein interaction networks analysis.
2020-01-09 | PXD016177 | Pride
Project description:One of the most common causes of coccidiosis in poultry
| PRJNA84153 | ENA
Project description:BackgroundChicken 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.ResultsWe 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.ConclusionEtv-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.
| S-EPMC5793433 | biostudies-literature