ArticleParasites & vectors2019
Characterization of protein arginine methyltransferase of TgPRMT5 in Toxoplasma gondii.
Article in Parasites & vectors, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Protein arginine methyltransferase 5 is essential for virulence in Toxoplasma gondii.Parasites & vectors · 2026Article
- Protein arginine methyltransferases in protozoan parasites: a new path for antiparasitic chemotherapy?Microbial cell (Graz, Austria) · 2026Article
- PRMT5 Inhibitor EPZ015666 Decreases the Viability and Encystment ofMolecules (Basel, Switzerland) · 2024Article
- Protein arginine methyltransferases in protozoan parasites.Parasitology · 2022Review
- Characterization of functions in parasite growth and virulence of four Toxoplasma gondii genes involved in lipid synthesis by CRISPR-Cas9 system.Parasitology research · 2021Article
- Review on the Current Trends of Toxoplasmosis Serodiagnosis in Humans.Frontiers in cellular and infection microbiology · 2020Review
- Characterization of the Role of Amylo-Alpha-1,6-Glucosidase Protein in the Infectivity ofFrontiers in cellular and infection microbiology · 2019Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundProtein arginine methylation is a prevalent post-translational modification. The protein arginine methyltransferase family (PRMT) is involved in many cellular processes in eukaryotes, including transcriptional regulation, epigenetic regulation, RNA metabolism, and DNA damage repair. Toxoplasma gondii, an opportunistic protozoan parasite, encodes five conserved PRMTs. PRMT5 is thought to be responsible for substantial PRMT activity in T. gondii; however, it has not yet been characterized.
methodsWe tagged the 3' end of the endogenous TgPRMT5 genomic locus with sequence encoding a 3X hemagglutinin (HA) epitope. IFA and WB were performed to check the expression and subcellular localization of TgPRMT5 in tachyzoites and bradyzoites. In vitro methylation assays were performed to determine whether endogenous TgPRMT5 has arginine methyltransferase activity.
resultsIFA and WB results showed that T. gondii PRMT5 (TgPRMT5) was localized in the cytoplasm in the tachyzoite stage; however, it shifts largely to the nuclear compartment in the bradyzoite stage. The in vitro methylation showed that TgPRMT5 has authentic type II PRMT activity and forms monomethylarginines and symmetric dimethylarginines.
conclusionsWe determined the expression and cellular localization of TgPRMT5 in tachyzoites and bradyzoites and confirmed its type II PRMT activity. We demonstrated the major changes in expression and cellular localization of TgPRMT5 during the tachyzoite and bradyzoite stages in T. gondii. Our findings suggest that TgPRMT5 protein may be involved in tachyzoite-bradyzoite transformation.
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