Evidence map›Paper›PMID 42231480›Full record

ArticleParasites & vectors2026

Protein arginine methyltransferase 5 is essential for virulence in Toxoplasma gondii.

Limei Xu, Huiru Liang, Shengchen Bai, Ruochen Xu, Bin Liu, Xiaohong Xu, Xinrong Xu, Min Liu

Abstract read
In one paragraph

Article in Parasites & vectors, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Limei Xu *Institute of Tropical Medicine, Department of Pathogen Biology, School of Public Health, Southern Medical University, Guangdong Provincial Key Laboratory of Tropical Disease Research, Key Laboratory of Prevention and Control for Emerging Infectious Diseases of Guangdong Higher Institutes, Key Laboratory of Infectious Diseases Research in South China, Ministry of Education, Guangzhou, 510515, Guangdong, China.
Huiru Liang *Institute of Tropical Medicine, Department of Pathogen Biology, School of Public Health, Southern Medical University, Guangdong Provincial Key Laboratory of Tropical Disease Research, Key Laboratory of Prevention and Control for Emerging Infectious Diseases of Guangdong Higher Institutes, Key Laboratory of Infectious Diseases Research in South China, Ministry of Education, Guangzhou, 510515, Guangdong, China.
Shengchen Bai *Institute of Tropical Medicine, Department of Pathogen Biology, School of Public Health, Southern Medical University, Guangdong Provincial Key Laboratory of Tropical Disease Research, Key Laboratory of Prevention and Control for Emerging Infectious Diseases of Guangdong Higher Institutes, Key Laboratory of Infectious Diseases Research in South China, Ministry of Education, Guangzhou, 510515, Guangdong, China.
Ruochen XuInstitute of Tropical Medicine, Department of Pathogen Biology, School of Public Health, Southern Medical University, Guangdong Provincial Key Laboratory of Tropical Disease Research, Key Laboratory of Prevention and Control for Emerging Infectious Diseases of Guangdong Higher Institutes, Key Laboratory of Infectious Diseases Research in South China, Ministry of Education, Guangzhou, 510515, Guangdong, China.
Bin LiuDepartment of Traditional Chinese Medicine, The Second Affiliated Hospital of Guangzhou Medical University, Guangzhou, 510515, Guangdong, China.
Xiaohong XuInstitute of Tropical Medicine, Department of Pathogen Biology, School of Public Health, Southern Medical University, Guangdong Provincial Key Laboratory of Tropical Disease Research, Key Laboratory of Prevention and Control for Emerging Infectious Diseases of Guangdong Higher Institutes, Key Laboratory of Infectious Diseases Research in South China, Ministry of Education, Guangzhou, 510515, Guangdong, China.
Xinrong XuInstitute of Tropical Medicine, Department of Pathogen Biology, School of Public Health, Southern Medical University, Guangdong Provincial Key Laboratory of Tropical Disease Research, Key Laboratory of Prevention and Control for Emerging Infectious Diseases of Guangdong Higher Institutes, Key Laboratory of Infectious Diseases Research in South China, Ministry of Education, Guangzhou, 510515, Guangdong, China.
Min LiuInstitute of Tropical Medicine, Department of Pathogen Biology, School of Public Health, Southern Medical University, Guangdong Provincial Key Laboratory of Tropical Disease Research, Key Laboratory of Prevention and Control for Emerging Infectious Diseases of Guangdong Higher Institutes, Key Laboratory of Infectious Diseases Research in South China, Ministry of Education, Guangzhou, 510515, Guangdong, China. ichbinlm@163.com.

Funding

Guangdong Provincial Natural Science Foundation 2021A1515011707
6 · The paper itself

Abstract

backgroundProtein arginine methyltransferase 5 (PRMT5) is a key enzyme responsible for catalyzing symmetric dimethylarginine (SDMA) modifications and plays crucial roles in epigenetic regulation, transcription, and cell cycle progression in eukaryotes. Although our previous study determined the expression and cellular localization of PRMT5 in tachyzoites and bradyzoites, and confirmed its type II PRMT activity, its functional significance in Toxoplasma gondii remains entirely uncharacterized.

methodsThis study aimed to explore the biological functions of PRMT5 in T. gondii. The prmt5 gene was disrupted in the type I RH strain using the clustered regularly interspaced short palindromic repeats (CRISPR) Cas9 system. The biological roles of PRMT5 were evaluated via multiple functional assays, including plaque formation, intracellular proliferation, host cell invasion, virulence, and tachyzoite to bradyzoite conversion assays. RNA sequencing was further performed to profile transcriptomic alterations induced by prmt5 disruption.

resultsPhenotypic characterization revealed that the ∆prmt5 strain exhibited reduced symmetric dimethylarginine (SDMA) levels as well as severe defects in plaque formation, invasion, intracellular replication, and bradyzoite differentiation. Accordingly, the virulence of the ∆prmt5 strain was dramatically attenuated, as all infected BALB/c mice survived over a 10-day period, in stark contrast to the 100% mortality observed in the wild-type control group within 10 days. RNA-sequencing analysis uncovered the molecular basis for these phenotypes, demonstrating that prmt5 disruption leads to global transcriptional dysregulation. Specifically, we identified a significant downregulation of genes associated with motor protein function and fatty acid metabolism pathways.

conclusionsOur research has demonstrated that PRMT5 plays a critical role in the proliferation, survival, pathogenicity, and regulation of gene expression in Toxoplasma gondii.

Indexed as

Protein-Arginine N-MethyltransferasesProtozoan ProteinsToxoplasmaAnimalsArginineCRISPR-Cas SystemsFemaleMiceMice, Inbred BALB CVirulenceArginineProtein-Arginine N-MethyltransferasesProtozoan ProteinsBradyzoite differentiationGene expressionProtein arginine methyltransferase 5Toxoplasma gondiiVirulence

Identifiers

PMID42231480
PMCPMC13445752

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.