{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T15:04:27Z","timestamp":1786115067876,"version":"build-2736575974"},"reference-count":43,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T00:00:00Z","timestamp":1780358400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2026,8,6]],"date-time":"2026-08-06T00:00:00Z","timestamp":1785974400000},"content-version":"vor","delay-in-days":65,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"DOI":"10.13039\/501100003453","name":"Guangdong Provincial Natural Science Foundation","doi-asserted-by":"crossref","award":["2021A1515011707"],"award-info":[{"award-number":["2021A1515011707"]}],"id":[{"id":"10.13039\/501100003453","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Parasites Vectors"],"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Background<\/jats:title>\n                    <jats:p>\n                      Protein 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\n                      <jats:italic>Toxoplasma gondii<\/jats:italic>\n                      remains entirely uncharacterized.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      This study aimed to explore the biological functions of PRMT5 in\n                      <jats:italic>T.\u00a0gondii<\/jats:italic>\n                      . The\n                      <jats:italic>prmt5<\/jats:italic>\n                      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\n                      <jats:italic>prmt5<\/jats:italic>\n                      disruption.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Phenotypic characterization revealed that the \u2206\n                      <jats:italic>prmt5<\/jats:italic>\n                      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 \u2206\n                      <jats:italic>prmt5<\/jats:italic>\n                      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\u00a0days. RNA-sequencing analysis uncovered the molecular basis for these phenotypes, demonstrating that\n                      <jats:italic>prmt5<\/jats:italic>\n                      disruption leads to global transcriptional dysregulation. Specifically, we identified a significant downregulation of genes associated with motor protein function and fatty acid metabolism pathways.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>\n                      Our research has demonstrated that PRMT5 plays a critical role in the proliferation, survival, pathogenicity, and regulation of gene expression in\n                      <jats:italic>Toxoplasma gondii<\/jats:italic>\n                      .\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1186\/s13071-026-07473-3","type":"journal-article","created":{"date-parts":[[2026,6,2]],"date-time":"2026-06-02T14:26:09Z","timestamp":1780410369000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Protein arginine methyltransferase 5 is essential for virulence in Toxoplasma gondii"],"prefix":"10.1186","volume":"19","author":[{"given":"Limei","family":"Xu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huiru","family":"Liang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shengchen","family":"Bai","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruochen","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bin","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaohong","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinrong","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,6,2]]},"reference":[{"key":"7473_CR1","doi-asserted-by":"publisher","first-page":"e00115","DOI":"10.1128\/CMR.00115-19","volume":"34","author":"HM Elsheikha","year":"2020","unstructured":"Elsheikha HM, Marra CM, Zhu X-Q. Epidemiology, pathophysiology, diagnosis, and management of cerebral toxoplasmosis. Clin Microbiol Rev. 2020;34:e00115-e119. https:\/\/doi.org\/10.1128\/CMR.00115-19.","journal-title":"Clin Microbiol Rev"},{"key":"7473_CR2","doi-asserted-by":"publisher","DOI":"10.3389\/fcimb.2018.00300","volume":"8","author":"M-J Bai","year":"2018","unstructured":"Bai M-J, Wang J-L, Elsheikha HM, Liang Q-L, Chen K, Nie L-B, et\u00a0al. Functional characterization of dense granule proteins in Toxoplasma gondii RH strain using CRISPR-Cas9 system. Front Cell Infect Microbiol. 2018;8:300. https:\/\/doi.org\/10.3389\/fcimb.2018.00300.","journal-title":"Front Cell Infect Microbiol"},{"key":"7473_CR3","doi-asserted-by":"publisher","first-page":"e177","DOI":"10.1016\/S2352-3018(17)30005-X","volume":"4","author":"Z-D Wang","year":"2017","unstructured":"Wang Z-D, Wang S-C, Liu H-H, Ma H-Y, Li Z-Y, Wei F, et\u00a0al. Prevalence and burden of Toxoplasma gondii infection in HIV-infected people: a systematic review and meta-analysis. Lancet HIV. 2017;4:e177\u201388. https:\/\/doi.org\/10.1016\/S2352-3018(17)30005-X.","journal-title":"Lancet HIV"},{"key":"7473_CR4","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1007\/s10393-019-01405-7","volume":"16","author":"AA Aguirre","year":"2019","unstructured":"Aguirre AA, Longcore T, Barbieri M, Dabritz H, Hill D, Klein PN, et\u00a0al. The one health approach to toxoplasmosis: epidemiology, control, and prevention strategies. EcoHealth. 2019;16:378\u201390. https:\/\/doi.org\/10.1007\/s10393-019-01405-7.","journal-title":"EcoHealth"},{"key":"7473_CR5","doi-asserted-by":"publisher","first-page":"3095","DOI":"10.1080\/21505594.2021.2012346","volume":"12","author":"SG Sanchez","year":"2021","unstructured":"Sanchez SG, Besteiro S. The pathogenicity and virulence of Toxoplasma gondii. Virulence. 2021;12:3095\u2013114. https:\/\/doi.org\/10.1080\/21505594.2021.2012346.","journal-title":"Virulence"},{"key":"7473_CR6","doi-asserted-by":"publisher","DOI":"10.3389\/fvets.2022.972500","volume":"9","author":"Y Jiang","year":"2022","unstructured":"Jiang Y, Shi Y, Hu D, Song X. The anti-toxoplasma activity of the plant natural phenolic compound piceatannol. Front Vet Sci. 2022;9:972500. https:\/\/doi.org\/10.3389\/fvets.2022.972500.","journal-title":"Front Vet Sci"},{"key":"7473_CR7","doi-asserted-by":"publisher","DOI":"10.1016\/j.preteyeres.2020.100882","volume":"81","author":"JR Smith","year":"2021","unstructured":"Smith JR, Ashander LM, Arruda SL, Cordeiro CA, Lie S, Rochet E, et\u00a0al. Pathogenesis of ocular toxoplasmosis. Prog Retin Eye Res. 2021;81:100882. https:\/\/doi.org\/10.1016\/j.preteyeres.2020.100882.","journal-title":"Prog Retin Eye Res"},{"key":"7473_CR8","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1111\/mmi.13867","volume":"107","author":"RR Yakubu","year":"2018","unstructured":"Yakubu RR, Weiss LM, Silmon De Monerri NC. Post\u2010translational modifications as key regulators of apicomplexan biology: insights from proteome\u2010wide studies. Mol Microbiol. 2018;107:1\u201323. https:\/\/doi.org\/10.1111\/mmi.13867.","journal-title":"Mol Microbiol"},{"key":"7473_CR9","doi-asserted-by":"publisher","DOI":"10.3892\/ijo.2023.5510","volume":"62","author":"K Wu","year":"2023","unstructured":"Wu K, Niu C, Liu H, Fu L. Research progress on PRMTs involved in epigenetic modification and tumour signalling pathway regulation (Review). Int J Oncol. 2023;62:62. https:\/\/doi.org\/10.3892\/ijo.2023.5510.","journal-title":"Int J Oncol"},{"key":"7473_CR10","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1517\/13543784.2016.1144747","volume":"25","author":"H Hu","year":"2016","unstructured":"Hu H, Qian K, Ho M-C, Zheng YG. Small molecule inhibitors of protein arginine methyltransferases. Expert Opin Investig Drugs. 2016;25:335\u201358. https:\/\/doi.org\/10.1517\/13543784.2016.1144747.","journal-title":"Expert Opin Investig Drugs"},{"key":"7473_CR11","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1016\/j.molcel.2016.11.003","volume":"65","author":"RS Blanc","year":"2017","unstructured":"Blanc RS, Richard S. Arginine methylation: the coming of age. Mol Cell. 2017;65:8\u201324. https:\/\/doi.org\/10.1016\/j.molcel.2016.11.003.","journal-title":"Mol Cell"},{"key":"7473_CR12","doi-asserted-by":"publisher","first-page":"509","DOI":"10.1038\/s41573-021-00159-8","volume":"20","author":"Q Wu","year":"2021","unstructured":"Wu Q, Schapira M, Arrowsmith CH, Barsyte-Lovejoy D. Protein arginine methylation: from enigmatic functions to therapeutic targeting. Nat Rev Drug Discov. 2021;20:509\u201330. https:\/\/doi.org\/10.1038\/s41573-021-00159-8.","journal-title":"Nat Rev Drug Discov"},{"key":"7473_CR13","doi-asserted-by":"publisher","first-page":"5413","DOI":"10.1021\/acs.chemrev.5b00003","volume":"115","author":"J Fuhrmann","year":"2015","unstructured":"Fuhrmann J, Clancy KW, Thompson PR. Chemical biology of protein arginine modifications in epigenetic regulation. Chem Rev. 2015;115:5413\u201361. https:\/\/doi.org\/10.1021\/acs.chemrev.5b00003.","journal-title":"Chem Rev"},{"key":"7473_CR14","doi-asserted-by":"publisher","first-page":"642","DOI":"10.1038\/s41580-019-0155-x","volume":"20","author":"E Guccione","year":"2019","unstructured":"Guccione E, Richard S. The regulation, functions and clinical relevance of arginine methylation. Nat Rev Mol Cell Biol. 2019;20:642\u201357. https:\/\/doi.org\/10.1038\/s41580-019-0155-x.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"7473_CR15","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1074\/mcp.M117.066951","volume":"16","author":"RR Yakubu","year":"2017","unstructured":"Yakubu RR, Silmon De Monerri NC, Nieves E, Kim K, Weiss LM. Comparative monomethylarginine proteomics suggests that protein arginine methyltransferase 1 (PRMT1) is a significant contributor to arginine monomethylation in Toxoplasma gondii. Mol Cell Proteomics. 2017;16:567\u201380. https:\/\/doi.org\/10.1074\/mcp.M117.066951.","journal-title":"Mol Cell Proteomics"},{"key":"7473_CR16","doi-asserted-by":"publisher","first-page":"1013","DOI":"10.1128\/EC.05103-11","volume":"10","author":"JC Fisk","year":"2011","unstructured":"Fisk JC, Read LK. Protein arginine methylation in parasitic protozoa. Eukaryot Cell. 2011;10:1013\u201322. https:\/\/doi.org\/10.1128\/EC.05103-11.","journal-title":"Eukaryot Cell"},{"key":"7473_CR17","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1017\/S0031182021002043","volume":"149","author":"MA Rodriguez","year":"2022","unstructured":"Rodriguez MA. Protein arginine methyltransferases in protozoan parasites. Parasitology. 2022;149:427\u201335. https:\/\/doi.org\/10.1017\/S0031182021002043.","journal-title":"Parasitology"},{"key":"7473_CR18","doi-asserted-by":"publisher","first-page":"932","DOI":"10.1111\/j.1742-4658.2012.08490.x","volume":"279","author":"Y Wang","year":"2012","unstructured":"Wang Y, Li C. Evolutionarily conserved protein arginine methyltransferases in non\u2010mammalian animal systems. FEBS J. 2012;279:932\u201345. https:\/\/doi.org\/10.1111\/j.1742-4658.2012.08490.x.","journal-title":"FEBS J"},{"key":"7473_CR19","doi-asserted-by":"publisher","first-page":"452","DOI":"10.1038\/embor.2008.45","volume":"9","author":"M Lacroix","year":"2008","unstructured":"Lacroix M, Messaoudi SE, Rodier G, Le Cam A, Sardet C, Fabbrizio E. The histone\u2010binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. EMBO Rep. 2008;9:452\u20138. https:\/\/doi.org\/10.1038\/embor.2008.45.","journal-title":"EMBO Rep"},{"key":"7473_CR20","doi-asserted-by":"publisher","first-page":"2041","DOI":"10.1007\/s00018-015-1847-9","volume":"72","author":"N Stopa","year":"2015","unstructured":"Stopa N, Krebs JE, Shechter D. The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond. Cell Mol Life Sci. 2015;72:2041\u201359. https:\/\/doi.org\/10.1007\/s00018-015-1847-9.","journal-title":"Cell Mol Life Sci"},{"key":"7473_CR21","doi-asserted-by":"publisher","DOI":"10.3390\/life11101074","volume":"11","author":"A Motolani","year":"2021","unstructured":"Motolani A, Martin M, Sun M, Lu T. The structure and functions of PRMT5 in human diseases. Life. 2021;11:1074. https:\/\/doi.org\/10.3390\/life11101074.","journal-title":"Life"},{"key":"7473_CR22","doi-asserted-by":"publisher","first-page":"212","DOI":"10.1111\/j.1365-2958.2008.06519.x","volume":"71","author":"CF Sautel","year":"2009","unstructured":"Sautel CF, Ortet P, Saksouk N, Kieffer S, Garin J, Bastien O, et\u00a0al. The histone methylase KMTox interacts with the redox\u2010sensor peroxiredoxin\u20101 and targets genes involved in Toxoplasma gondii antioxidant defences. Mol Microbiol. 2009;71:212\u201326. https:\/\/doi.org\/10.1111\/j.1365-2958.2008.06519.x.","journal-title":"Mol Microbiol"},{"key":"7473_CR23","doi-asserted-by":"publisher","first-page":"413","DOI":"10.1111\/j.1462-5822.2010.01446.x","volume":"12","author":"A Bougdour","year":"2010","unstructured":"Bougdour A, Braun L, Cannella D, Hakimi M-A. Chromatin modifications: implications in the regulation of gene expression in Toxoplasma gondii. Cell Microbiol. 2010;12:413\u201323. https:\/\/doi.org\/10.1111\/j.1462-5822.2010.01446.x.","journal-title":"Cell Microbiol"},{"key":"7473_CR24","doi-asserted-by":"publisher","DOI":"10.1186\/s13071-019-3464-1","volume":"12","author":"M Liu","year":"2019","unstructured":"Liu M, Li F-X, Li C-Y, Li X-C, Chen L-F, Wu K, et\u00a0al. Characterization of protein arginine methyltransferase of TgPRMT5 in Toxoplasma gondii. Parasit Vectors. 2019;12:221. https:\/\/doi.org\/10.1186\/s13071-019-3464-1.","journal-title":"Parasit Vectors"},{"key":"7473_CR25","doi-asserted-by":"publisher","first-page":"1126","DOI":"10.7150\/ijbs.21247","volume":"13","author":"C He","year":"2017","unstructured":"He C, Kong L, Zhou L, Xia J, Wei H, Liu M, et\u00a0al. Host cell vimentin restrains Toxoplasma gondii invasion and phosphorylation of vimentin is partially regulated by interaction with Tg ROP18. Int J Biol Sci. 2017;13:1126\u201337. https:\/\/doi.org\/10.7150\/ijbs.21247.","journal-title":"Int J Biol Sci"},{"key":"7473_CR26","doi-asserted-by":"publisher","unstructured":"Mayoral J, Di Cristina M, Carruthers VB, Weiss LM. Toxoplasma gondii: bradyzoite differentiation in vitro and in vivo. In: Tonkin CJ, editor. Toxoplasma gondii [Internet]. Springer US, New York, NY; 2020 [cited 2025 Oct 10]. pp. 269\u201382. https:\/\/doi.org\/10.1007\/978-1-4939-9857-9_15","DOI":"10.1007\/978-1-4939-9857-9_15"},{"key":"7473_CR27","doi-asserted-by":"publisher","first-page":"210","DOI":"10.1016\/j.jprot.2013.07.010","volume":"91","author":"K Lott","year":"2013","unstructured":"Lott K, Li J, Fisk JC, Wang H, Aletta JM, Qu J, et\u00a0al. Global proteomic analysis in trypanosomes reveals unique proteins and conserved cellular processes impacted by arginine methylation. J Proteomics. 2013;91:210\u201325. https:\/\/doi.org\/10.1016\/j.jprot.2013.07.010.","journal-title":"J Proteomics"},{"key":"7473_CR28","doi-asserted-by":"publisher","first-page":"1625","DOI":"10.1084\/jem.20020258","volume":"195","author":"A Barragan","year":"2002","unstructured":"Barragan A, Sibley LD. Transepithelial migration of Toxoplasma gondii is linked to parasite motility and virulence. J Exp Med. 2002;195:1625\u201333. https:\/\/doi.org\/10.1084\/jem.20020258.","journal-title":"J Exp Med"},{"key":"7473_CR29","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0085763","volume":"9","author":"JM Leung","year":"2014","unstructured":"Leung JM, Rould MA, Konradt C, Hunter CA, Ward GE. Disruption of TgPHIL1 alters specific parameters of Toxoplasma gondii motility measured in a quantitative, three-dimensional live motility assay. PLoS ONE. 2014;9:e85763. https:\/\/doi.org\/10.1371\/journal.pone.0085763.","journal-title":"PLoS ONE"},{"key":"7473_CR30","doi-asserted-by":"publisher","first-page":"837","DOI":"10.1126\/science.1074553","volume":"298","author":"M Meissner","year":"2002","unstructured":"Meissner M, Schl\u00fcter D, Soldati D. Role of Toxoplasma gondii Myosin A in powering parasite gliding and host cell invasion. Science. 2002;298:837\u201340. https:\/\/doi.org\/10.1126\/science.1074553.","journal-title":"Science"},{"key":"7473_CR31","doi-asserted-by":"publisher","first-page":"2149","DOI":"10.1093\/emboj\/21.9.2149","volume":"21","author":"A Herm-Gotz","year":"2002","unstructured":"Herm-Gotz A. Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor. EMBO J. 2002;21:2149\u201358. https:\/\/doi.org\/10.1093\/emboj\/21.9.2149.","journal-title":"EMBO J"},{"key":"7473_CR32","doi-asserted-by":"publisher","unstructured":"Williams MJ, Alonso H, Enciso M, Egarter S, Sheiner L, Meissner M, et al. Two essential light chains regulate the MyoA lever arm to promote Toxoplasma gliding motility. MBio. 2015;6(3):e00845-15. https:\/\/doi.org\/10.1128\/mbio.00845-15","DOI":"10.1128\/mbio.00845-15"},{"key":"7473_CR33","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.02094-15","volume":"7","author":"K El Bissati","year":"2016","unstructured":"El Bissati K, Suvorova ES, Xiao H, Lucas O, Upadhya R, Ma Y, et\u00a0al. Toxoplasma gondii arginine methyltransferase 1 (PRMT1) is necessary for centrosome dynamics during tachyzoite cell division. MBio. 2016;7:e02094-15. https:\/\/doi.org\/10.1128\/mBio.02094-15.","journal-title":"MBio"},{"key":"7473_CR34","doi-asserted-by":"publisher","first-page":"3108","DOI":"10.1093\/gbe\/evx231","volume":"9","author":"D Moog","year":"2017","unstructured":"Moog D, Przyborski JM, Maier UG. Genomic and proteomic evidence for the presence of a peroxisome in the apicomplexan parasite Toxoplasma gondii and other coccidia. Genome Biol Evol. 2017;9:3108\u201321. https:\/\/doi.org\/10.1093\/gbe\/evx231.","journal-title":"Genome Biol Evol"},{"key":"7473_CR35","doi-asserted-by":"publisher","first-page":"994","DOI":"10.1194\/jlr.M082891","volume":"59","author":"D Dubois","year":"2018","unstructured":"Dubois D, Fernandes S, Amiar S, Dass S, Katris NJ, Bott\u00e9 CY, et\u00a0al. Toxoplasma gondii acetyl-CoA synthetase is involved in fatty acid elongation (of long fatty acid chains) during tachyzoite life stages. J Lipid Res. 2018;59:994\u20131004. https:\/\/doi.org\/10.1194\/jlr.M082891.","journal-title":"J Lipid Res"},{"key":"7473_CR36","doi-asserted-by":"publisher","first-page":"4957","DOI":"10.1074\/jbc.m111.310144","volume":"287","author":"S Ramakrishnan","year":"2012","unstructured":"Ramakrishnan S, Docampo MD, MacRae JI, Pujol FM, Brooks CF, Van Dooren GG, et\u00a0al. Apicoplast and endoplasmic reticulum cooperate in fatty acid biosynthesis in apicomplexan parasite Toxoplasma gondii. J Biol Chem. 2012;287:4957\u201371. https:\/\/doi.org\/10.1074\/jbc.m111.310144.","journal-title":"J Biol Chem"},{"key":"7473_CR37","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/j.gendis.2019.06.002","volume":"6","author":"F Zhu","year":"2019","unstructured":"Zhu F, Rui L. PRMT5 in gene regulation and hematologic malignancies. Genes Dis. 2019;6:247\u201357. https:\/\/doi.org\/10.1016\/j.gendis.2019.06.002.","journal-title":"Genes Dis"},{"key":"7473_CR38","doi-asserted-by":"publisher","first-page":"621","DOI":"10.1016\/j.chom.2015.10.014","volume":"18","author":"NC Silmon de Monerri","year":"2015","unstructured":"Silmon de Monerri NC, Yakubu RR, Chen AL, Bradley PJ, Nieves E, Weiss LM, et\u00a0al. The ubiquitin proteome of Toxoplasma gondii reveals roles for protein ubiquitination in cell-cycle transitions. Cell Host Microbe. 2015;18:621\u201333. https:\/\/doi.org\/10.1016\/j.chom.2015.10.014.","journal-title":"Cell Host Microbe"},{"key":"7473_CR39","doi-asserted-by":"publisher","first-page":"6871","DOI":"10.1073\/pnas.1300059110","volume":"110","author":"JB Radke","year":"2013","unstructured":"Radke JB, Lucas O, De Silva EK, Ma Y, Sullivan WJ, Weiss LM, et\u00a0al. ApiAP2 transcription factor restricts development of the Toxoplasma tissue cyst. Proc Natl Acad Sci USA. 2013;110:6871\u20136. https:\/\/doi.org\/10.1073\/pnas.1300059110.","journal-title":"Proc Natl Acad Sci USA"},{"key":"7473_CR40","doi-asserted-by":"publisher","DOI":"10.1128\/mSphere.00347-16","volume":"2","author":"D-P Hong","year":"2017","unstructured":"Hong D-P, Radke JB, White MW. Opposing transcriptional mechanisms regulate Toxoplasma development. mSphere. 2017;2:e00347-16. https:\/\/doi.org\/10.1128\/mSphere.00347-16.","journal-title":"mSphere"},{"key":"7473_CR41","doi-asserted-by":"publisher","DOI":"10.1128\/mSphere.00054-17","volume":"2","author":"S Huang","year":"2017","unstructured":"Huang S, Holmes MJ, Radke JB, Hong D-P, Liu T-K, White MW, et\u00a0al. Toxoplasma gondii AP2IX-4 regulates gene expression during bradyzoite development. mSphere. 2017;2:e00054-17. https:\/\/doi.org\/10.1128\/mSphere.00054-17.","journal-title":"mSphere"},{"key":"7473_CR42","doi-asserted-by":"publisher","DOI":"10.3390\/ani15091349","volume":"15","author":"L-X Sun","year":"2025","unstructured":"Sun L-X, Wang M, Elsheikha HM, Xie S-C, Fu B-Q, Zhu X-Q, et\u00a0al. AP2X-8 is important for tachyzoite growth and bradyzoite differentiation of Toxoplasma gondii. Animals Basel. 2025;15:1349. https:\/\/doi.org\/10.3390\/ani15091349.","journal-title":"Animals Basel"},{"key":"7473_CR43","doi-asserted-by":"publisher","first-page":"199","DOI":"10.15698\/cst2020.08.228","volume":"4","author":"H Kim","year":"2020","unstructured":"Kim H, Ronai ZA. PRMT5 function and targeting in cancer. CST. 2020;4:199\u2013215. https:\/\/doi.org\/10.15698\/cst2020.08.228.","journal-title":"CST"}],"container-title":["Parasites &amp; Vectors"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s13071-026-07473-3","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13071-026-07473-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s13071-026-07473-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,6]],"date-time":"2026-08-06T00:06:36Z","timestamp":1785974796000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1186\/s13071-026-07473-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,2]]},"references-count":43,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2026,12]]}},"alternative-id":["7473"],"URL":"https:\/\/doi.org\/10.1186\/s13071-026-07473-3","relation":{},"ISSN":["1756-3305"],"issn-type":[{"value":"1756-3305","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,2]]},"assertion":[{"value":"17 December 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 May 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"2 June 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The study was performed in a standard SPF environment in accordance with the animal welfare and related ethical requirements of the Animal Ethics Committee of Guangdong Provincial Medical Animal Center (GY-2024-765).","order":1,"name":"Ethics","label":"Ethics approval and consent to participate","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","label":"Consent for publication","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":3,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"317"}}