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Updated: May 3, 2026

A Non-Coding Small RNA MicC Contributes to Virulence in Outer Membrane Proteins in Salmonella Enteritidis
Published on: January 27, 2021
Eimeria tenella rhomboid 3 has a potential role in microneme protein cleavage
Jun Zheng1, Pengtao Gong2, Honglin Jia3
1Key Laboratory of Zoonosis, Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, China; National Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China.
Abstract:
Invasion in several apicomplexan parasites, including Eimeria tenella, is accompanied by shedding of surface adhesins by intramembrane proteolysis mediated by rhomboid protease. We have previously identified E. tenella rhomboid 3 (EtROM3), but its precise role has not been elucidated. In this study, the interactions between EtROM3 and microneme (MIC) proteins were analyzed using the yeast two hybrid technique. The results showed that c-Myc-ROM3 fusion protein interacted with EtMIC4 protein in co-transformed AH109 yeasts, which was further confirmed by immunoprecipitation assay. Smaller EtMIC4 band from co-transformed cells suggested that EtROM3 was an active protease and involved in the cleavage of EtMIC4.
Insights
Eimeria tenella rhomboid 3 (EtROM3) protease cleaves the EtMIC4 surface protein during parasite invasion. This study confirms EtROM3
Area of Science:
- Parasitology
- Molecular Biology
- Cell Biology
Background:
- Apicomplexan parasite invasion involves shedding surface adhesins.
- Rhomboid proteases mediate this shedding via intramembrane proteolysis.
- The specific role of E. tenella rhomboid 3 (EtROM3) remains unclear.
Purpose of the Study:
- To investigate the interactions between EtROM3 and microneme (MIC) proteins.
- To elucidate the function of EtROM3 in Eimeria tenella.
Main Methods:
- Yeast two-hybrid technique to analyze protein interactions.
- Co-immunoprecipitation assays to confirm interactions.
- Analysis of protein cleavage patterns.
Main Results:
- EtROM3 was found to interact with the EtMIC4 protein.
- Confirmation of EtROM3 and EtMIC4 interaction via immunoprecipitation.
- Evidence suggests EtROM3 is an active protease that cleaves EtMIC4.
Conclusions:
- EtROM3 plays a role in the invasion process of Eimeria tenella.
- EtROM3 is involved in the proteolytic cleavage of EtMIC4.
- Understanding EtROM3 function could reveal new targets for antiparasitic strategies.
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