{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,10]],"date-time":"2026-11-10T15:27:07Z","timestamp":1794324427410,"version":"4.9.0"},"reference-count":56,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,5,6]],"date-time":"2024-05-06T00:00:00Z","timestamp":1714953600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2024,5,6]],"date-time":"2024-05-06T00:00:00Z","timestamp":1714953600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Commun"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Infection with the apicomplexan protozoan <jats:italic>Toxoplasma gondii<\/jats:italic> can be life-threatening in immunocompromised hosts. Transmission frequently occurs through the oral ingestion of <jats:italic>T. gondii<\/jats:italic> bradyzoite cysts, which transition to tachyzoites, disseminate, and then form cysts containing bradyzoites in the central nervous system, resulting in latent infection. Encapsulation of bradyzoites by a cyst wall is critical for immune evasion, survival, and transmission. O-glycosylation of the protein CST1 by the mucin-type O-glycosyltransferase <jats:italic>T. gondii<\/jats:italic> (Txg<jats:italic>)<\/jats:italic> GalNAc-T3 influences cyst wall rigidity and stability. Here, we report X-ray crystal structures of TxgGalNAc-T3, revealing multiple features that are strictly conserved among its apicomplexan homologues. This includes a unique 2<jats:sup>nd<\/jats:sup> metal that is coupled to substrate binding and enzymatic activity in vitro and cyst wall O-glycosylation in <jats:italic>T. gondii<\/jats:italic>. The study illustrates the divergence of pathogenic protozoan GalNAc-Ts from their host homologues and lays the groundwork for studying apicomplexan GalNAc-Ts as therapeutic targets in disease.<\/jats:p>","DOI":"10.1038\/s41467-024-48253-w","type":"journal-article","created":{"date-parts":[[2024,5,6]],"date-time":"2024-05-06T18:02:41Z","timestamp":1715018561000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["A Toxoplasma gondii O-glycosyltransferase that modulates bradyzoite cyst wall rigidity is distinct from host homologues"],"prefix":"10.1038","volume":"15","author":[{"given":"Pranav","family":"Kumar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tadakimi","family":"Tomita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7919-7613","authenticated-orcid":false,"given":"Thomas A.","family":"Gerken","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Collin J.","family":"Ballard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong Sok","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louis M.","family":"Weiss","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7152-2939","authenticated-orcid":false,"given":"Nadine L.","family":"Samara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,5,6]]},"reference":[{"key":"48253_CR1","doi-asserted-by":"publisher","first-page":"1965","DOI":"10.1016\/S0140-6736(04)16412-X","volume":"363","author":"JG Montoya","year":"2004","unstructured":"Montoya, J. G. & Liesenfeld, O. Toxoplasmosis. Lancet 363, 1965\u20131976 (2004).","journal-title":"Lancet"},{"key":"48253_CR2","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1016\/j.ijmm.2014.09.002","volume":"304","author":"D Schluter","year":"2014","unstructured":"Schluter, D. et al. Animals are key to human toxoplasmosis. Int. J. Med. Microbiol. 304, 917\u2013929 (2014).","journal-title":"Int. J. Med. Microbiol."},{"key":"48253_CR3","doi-asserted-by":"publisher","first-page":"S106","DOI":"10.1093\/cid\/cix1139","volume":"66","author":"N Ford","year":"2018","unstructured":"Ford, N. et al. Managing advanced hiv disease in a public health approach. Clin. Infect. Dis. 66, S106\u2013SS110 (2018).","journal-title":"Clin. Infect. Dis."},{"key":"48253_CR4","doi-asserted-by":"publisher","first-page":"273","DOI":"10.2147\/DDDT.S60973","volume":"11","author":"PH Alday","year":"2017","unstructured":"Alday, P. H. & Doggett, J. S. Drugs in development for toxoplasmosis: advances, challenges, and current status. Drug Des. Devel. Ther. 11, 273\u2013293 (2017).","journal-title":"Drug Des. Devel. Ther."},{"key":"48253_CR5","doi-asserted-by":"publisher","first-page":"7183","DOI":"10.1111\/febs.16148","volume":"288","author":"HH Wandall","year":"2021","unstructured":"Wandall, H. H., Nielsen, M. A. I., King-Smith, S., de Haan, N. & Bagdonaite, I. Global functions of O-glycosylation: promises and challenges in O-glycobiology. FEBS J. 288, 7183\u20137212 (2021).","journal-title":"FEBS J."},{"key":"48253_CR6","doi-asserted-by":"publisher","first-page":"100024","DOI":"10.1074\/mcp.R120.002263","volume":"20","author":"CM West","year":"2021","unstructured":"West, C. M., Malzl, D., Hykollari, A. & Wilson, I. B. H. Glycomics, Glycoproteomics, and Glycogenomics: An Inter-Taxa Evolutionary Perspective. Mol. Cell Proteomics 20, 100024 (2021).","journal-title":"Mol. Cell Proteomics"},{"key":"48253_CR7","doi-asserted-by":"publisher","first-page":"e1003823","DOI":"10.1371\/journal.ppat.1003823","volume":"9","author":"T Tomita","year":"2013","unstructured":"Tomita, T. et al. The Toxoplasma gondii cyst wall protein CST1 is critical for cyst wall integrity and promotes bradyzoite persistence. PLoS Pathog 9, e1003823 (2013).","journal-title":"PLoS Pathog"},{"key":"48253_CR8","doi-asserted-by":"publisher","first-page":"2457","DOI":"10.1007\/s00436-018-5934-3","volume":"117","author":"T Tomita","year":"2018","unstructured":"Tomita, T., Ma, Y. & Weiss, L. Characterization of a SRS13: a new cyst wall mucin-like domain containing protein. Parasitol. Res. 117, 2457\u20132466 (2018).","journal-title":"Parasitol. Res."},{"key":"48253_CR9","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1016\/j.molbiopara.2009.10.006","volume":"169","author":"MP Craver","year":"2010","unstructured":"Craver, M. P., Rooney, P. J. & Knoll, L. J. Isolation of Toxoplasma gondii development mutants identifies a potential proteophosphogylcan that enhances cyst wall formation. Mol Biochem Parasitol 169, 120\u2013123 (2010).","journal-title":"Mol Biochem Parasitol"},{"key":"48253_CR10","doi-asserted-by":"publisher","first-page":"241","DOI":"10.1016\/S0166-6851(98)00136-4","volume":"97","author":"C Zinecker","year":"1998","unstructured":"Zinecker, C., Striepen, B., Tomavo, S., Dubremetz, J. & Schwartz, R. T. The dense granule antigen, GRA2 of Toxoplasma gondii is a glycoprotein containing O-linked oligosaccharides. Mol. Biochem. Parasitol. 97, 241\u2013246 (1998).","journal-title":"Mol. Biochem. Parasitol."},{"key":"48253_CR11","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1016\/j.ijpara.2003.12.004","volume":"34","author":"C Jung","year":"2004","unstructured":"Jung, C., Lee, C. Y. & Grigg, M. E. The SRS superfamily of Toxoplasma surface proteins. Int. J. Parasitol. 34, 285\u2013296 (2004).","journal-title":"Int. J. Parasitol."},{"key":"48253_CR12","doi-asserted-by":"publisher","first-page":"521","DOI":"10.1146\/annurev.biochem.76.061005.092322","volume":"77","author":"LL Lairson","year":"2008","unstructured":"Lairson, L. L., Henrissat, B., Davies, G. J. & Withers, S. G. Glycosyltransferases: structures, functions, and mechanisms. Annu. Rev. Biochem. 77, 521\u2013555 (2008).","journal-title":"Annu. Rev. Biochem."},{"key":"48253_CR13","doi-asserted-by":"publisher","first-page":"768","DOI":"10.1093\/glycob\/cwr183","volume":"22","author":"J Raman","year":"2012","unstructured":"Raman, J., Guan, Y., Perrine, C. L., Gerken, T. A. & Tabak, L. A. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases: completion of the family tree. Glycobiology 22, 768\u2013777 (2012).","journal-title":"Glycobiology"},{"key":"48253_CR14","doi-asserted-by":"publisher","first-page":"853","DOI":"10.1038\/s41589-019-0350-2","volume":"15","author":"KW Moremen","year":"2019","unstructured":"Moremen, K. W. & Haltiwanger, R. S. Emerging structural insights into glycosyltransferase-mediated synthesis of glycans. Nat. Chem. Biol. 15, 853\u2013864 (2019).","journal-title":"Nat. Chem. Biol."},{"key":"48253_CR15","doi-asserted-by":"publisher","first-page":"1490","DOI":"10.1002\/pro.5560050805","volume":"5","author":"B Hazes","year":"1996","unstructured":"Hazes, B. The (QxW)3 domain: a flexible lectin scaffold. Protein Sci. 5, 1490\u20131501 (1996).","journal-title":"Protein Sci."},{"key":"48253_CR16","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-018-05978-9","volume":"9","author":"S Ji","year":"2018","unstructured":"Ji, S. et al. A molecular switch orchestrates enzyme specificity and secretory granule morphology. Nat. Commun. 9, 3508 (2018).","journal-title":"Nat. Commun."},{"key":"48253_CR17","doi-asserted-by":"publisher","first-page":"351","DOI":"10.1038\/s41589-019-0444-x","volume":"16","author":"M de Las Rivas","year":"2020","unstructured":"de Las Rivas, M. et al. Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3. Nat. Chem. Biol. 16, 351\u2013360 (2020).","journal-title":"Nat. Chem. Biol."},{"key":"48253_CR18","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms7937","volume":"6","author":"E Lira-Navarrete","year":"2015","unstructured":"Lira-Navarrete, E. et al. Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation. Nat. Commun. 6, 6937 (2015).","journal-title":"Nat. Commun."},{"key":"48253_CR19","doi-asserted-by":"publisher","first-page":"20404","DOI":"10.1073\/pnas.1902211116","volume":"116","author":"AJ Fernandez","year":"2019","unstructured":"Fernandez, A. J. et al. The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function. Proc. Natl Acad. Sci. USA 116, 20404\u201320410 (2019).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"48253_CR20","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1093\/glycob\/cwv108","volume":"26","author":"L Revoredo","year":"2016","unstructured":"Revoredo, L. et al. Mucin-type O-glycosylation is controlled by short- and long-range glycopeptide substrate recognition that varies among members of the polypeptide GalNAc transferase family. Glycobiology 26, 360\u2013376 (2016).","journal-title":"Glycobiology"},{"key":"48253_CR21","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/S0166-6851(03)00196-8","volume":"131","author":"BS Wojczyk","year":"2003","unstructured":"Wojczyk, B. S. et al. cDNA cloning and expression of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase T1 from Toxoplasma gondii. Mol. Biochem. Parasitol. 131, 93\u2013107 (2003).","journal-title":"Mol. Biochem. Parasitol."},{"key":"48253_CR22","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.abb.2004.02.013","volume":"426","author":"MM Stwora-Wojczyk","year":"2004","unstructured":"Stwora-Wojczyk, M. M., Dzierszinski, F., Roos, D. S., Spitalnik, S. L. & Wojczyk, B. S. Functional characterization of a novel Toxoplasma gondii glycosyltransferase: UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3. Arch. Biochem. Biophys. 426, 231\u2013240 (2004).","journal-title":"Arch. Biochem. Biophys."},{"key":"48253_CR23","doi-asserted-by":"publisher","first-page":"309","DOI":"10.1016\/j.ijpara.2003.11.016","volume":"34","author":"MM Stwora-Wojczyk","year":"2004","unstructured":"Stwora-Wojczyk, M. M., Kissinger, J. C., Spitalnik, S. L. & Wojczyk, B. S. O-glycosylation in Toxoplasma gondii: identification and analysis of a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Int. J. Parasitol. 34, 309\u2013322 (2004).","journal-title":"Int. J. Parasitol."},{"key":"48253_CR24","doi-asserted-by":"crossref","unstructured":"Tomita, T. et al. Making Home Sweet and Sturdy: Toxoplasma gondii ppGalNAc-Ts Glycosylate in Hierarchical Order and Confer Cyst Wall Rigidity. mBio 8, 1\u201316 (2017).","DOI":"10.1128\/mBio.02048-16"},{"key":"48253_CR25","doi-asserted-by":"publisher","first-page":"1755","DOI":"10.1017\/S0031182019000040","volume":"146","author":"G Bandini","year":"2019","unstructured":"Bandini, G., Albuquerque-Wendt, A., Hegermann, J., Samuelson, J. & Routier, F. H. Protein O- and C-Glycosylation pathways in Toxoplasma gondii and Plasmodium falciparum. Parasitology 146, 1755\u20131766 (2019).","journal-title":"Parasitology"},{"key":"48253_CR26","doi-asserted-by":"publisher","first-page":"1104","DOI":"10.1074\/jbc.RA118.006072","volume":"294","author":"E Gas-Pascual","year":"2019","unstructured":"Gas-Pascual, E. et al. CRISPR\/Cas9 and glycomics tools for Toxoplasma glycobiology. J. Biol. Chem. 294, 1104\u20131125 (2019).","journal-title":"J. Biol. Chem."},{"key":"48253_CR27","doi-asserted-by":"publisher","first-page":"3","DOI":"10.1021\/acschembio.9b00619","volume":"15","author":"L Yakovlieva","year":"2020","unstructured":"Yakovlieva, L. & Walvoort, M. T. C. Processivity in Bacterial Glycosyltransferases. ACS Chem. Biol. 15, 3\u201316 (2020).","journal-title":"ACS Chem. Biol."},{"key":"48253_CR28","doi-asserted-by":"publisher","first-page":"15307","DOI":"10.1073\/pnas.0405657101","volume":"101","author":"TA Fritz","year":"2004","unstructured":"Fritz, T. A., Hurley, J. H., Trinh, L., Shiloach, J. & Tabak, L. A. The beginnings of mucin biosynthesis: The crystal structure of UDP-GalNAc:polypeptide \u2000-Nacetylgalactosaminyltransferase-T1. Proc. Natl Acad. Sci. USA 101, 15307\u201315312 (2004).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"48253_CR29","doi-asserted-by":"publisher","first-page":"8613","DOI":"10.1074\/jbc.M513590200","volume":"281","author":"TA Fritz","year":"2006","unstructured":"Fritz, T. A., Raman, J. & Tabak, L. A. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2. J. Biol. Chem. 281, 8613\u20138619 (2006).","journal-title":"J. Biol. Chem."},{"key":"48253_CR30","doi-asserted-by":"publisher","first-page":"708","DOI":"10.1016\/j.jmb.2006.03.061","volume":"359","author":"T Kubota","year":"2006","unstructured":"Kubota, T. et al. Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J. Mol. Biol. 359, 708\u2013727 (2006).","journal-title":"J. Mol. Biol."},{"key":"48253_CR31","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1016\/j.bbrc.2019.01.084","volume":"510","author":"C Yu","year":"2019","unstructured":"Yu, C., Liang, L. & Yin, Y. Structural basis of carbohydrate transfer activity of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase 7. Biochem. Biophys. Res. Commun. 510, 266\u2013271 (2019).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"48253_CR32","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-017-02006-0","volume":"8","author":"M de Las Rivas","year":"2017","unstructured":"de Las Rivas, M. et al. The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences. Nat. Commun. 8, 1959 (2017).","journal-title":"Nat. Commun."},{"key":"48253_CR33","doi-asserted-by":"publisher","first-page":"1274","DOI":"10.1021\/acscentsci.8b00488","volume":"4","author":"M de Las Rivas","year":"2018","unstructured":"de Las Rivas, M. et al. Structural and mechanistic insights into the catalytic-domain-mediated short-range glycosylation preferences of GalNAc-T4. ACS Cent. Sci. 4, 1274\u20131290 (2018).","journal-title":"ACS Cent. Sci."},{"key":"48253_CR34","doi-asserted-by":"publisher","first-page":"22942","DOI":"10.1074\/jbc.M803387200","volume":"283","author":"J Raman","year":"2008","unstructured":"Raman, J. et al. The catalytic and lectin domains of UDP-GalNAc:polypeptide alpha-N-Acetylgalactosaminyltransferase function in concert to direct glycosylation site selection. J. Biol. Chem. 283, 22942\u201322951 (2008).","journal-title":"J. Biol. Chem."},{"key":"48253_CR35","doi-asserted-by":"publisher","first-page":"5249","DOI":"10.1016\/S0021-9258(19)57206-4","volume":"261","author":"A Elhammer","year":"1986","unstructured":"Elhammer, A. & Kornfeld, S. Purification and characterization ofu dp-n-acetylgalactosamine:polypeptide n-acetylgalactosaminyltransferase from bovine colostrum and murine lymphomaB W5147 Cells. J. Biol. Chem. 261, 5249\u20135255 (1986).","journal-title":"J. Biol. Chem."},{"key":"48253_CR36","doi-asserted-by":"publisher","first-page":"19637","DOI":"10.1074\/jbc.M114.565390","volume":"289","author":"DA Pace","year":"2014","unstructured":"Pace, D. A., McKnight, C. A., Liu, J., Jimenez, V. & Moreno, S. N. Calcium entry in Toxoplasma gondii and its enhancing effect of invasion-linked traits. J. Biol. Chem. 289, 19637\u201319647 (2014).","journal-title":"J. Biol. Chem."},{"key":"48253_CR37","doi-asserted-by":"publisher","first-page":"105771","DOI":"10.1016\/j.jbc.2024.105771","volume":"300","author":"MA Hortua Triana","year":"2024","unstructured":"Hortua Triana, M. A., Marquez-Nogueras, K. M., Fazli, M. S., Quinn, S. & Moreno, S. N. J. Regulation of calcium entry by cyclic GMP signaling in Toxoplasma gondii. J. Biol. Chem. 300, 105771 (2024).","journal-title":"J. Biol. Chem."},{"key":"48253_CR38","doi-asserted-by":"publisher","first-page":"8206","DOI":"10.1002\/anie.201402781","volume":"53","author":"E Lira-Navarrete","year":"2014","unstructured":"Lira-Navarrete, E. et al. Substrate-guided front-face reaction revealed by combined structural snapshots and metadynamics for the polypeptide N-acetylgalactosaminyltransferase 2. Angew Chem. Int. Ed. Engl. 53, 8206\u20138210 (2014).","journal-title":"Angew Chem. Int. Ed. Engl."},{"key":"48253_CR39","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-33988-1","volume":"13","author":"TJB Forrester","year":"2022","unstructured":"Forrester, T. J. B. et al. The retaining beta-Kdo glycosyltransferase WbbB uses a double-displacement mechanism with an intermediate adduct rearrangement step. Nat. Commun. 13, 6277 (2022).","journal-title":"Nat. Commun."},{"key":"48253_CR40","doi-asserted-by":"publisher","first-page":"104609","DOI":"10.1016\/j.jbc.2023.104609","volume":"299","author":"L Doyle","year":"2023","unstructured":"Doyle, L. et al. Mechanism and linkage specificities of the dual retaining beta-Kdo glycosyltransferase modules of KpsC from bacterial capsule biosynthesis. J. Biol. Chem. 299, 104609 (2023).","journal-title":"J. Biol. Chem."},{"key":"48253_CR41","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-36598-7","volume":"14","author":"DM Sorensen","year":"2023","unstructured":"Sorensen, D. M. et al. Identification of global inhibitors of cellular glycosylation. Nat. Commun. 14, 948 (2023).","journal-title":"Nat. Commun."},{"key":"48253_CR42","doi-asserted-by":"crossref","unstructured":"Song, L. & Linstedt, A. D. Inhibitor of ppGalNAc-T3-mediated O-glycosylation blocks cancer cell invasiveness and lowers FGF23 levels. Elife 6, 1\u201315 (2017).","DOI":"10.7554\/eLife.24051"},{"key":"48253_CR43","doi-asserted-by":"crossref","unstructured":"Otwinowski, Z. & Minor, W. Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology, Carter, C. W., Jr. & Sweet, R. M. Eds., Academic Press (New York). 276, 307\u2013326 (1997).","DOI":"10.1016\/S0076-6879(97)76066-X"},{"key":"48253_CR44","doi-asserted-by":"publisher","first-page":"1131","DOI":"10.1107\/S0907444903008126","volume":"59","author":"E Potterton","year":"2003","unstructured":"Potterton, E., Briggs, P., Turkenburg, M. & Dodson, E. A graphical user interface to the CCP4 program suite. Acta Crystallogr. D. Biol. Crystallogr. 59, 1131\u20131137 (2003).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"48253_CR45","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S0907444910045749","volume":"67","author":"MD Winn","year":"2011","unstructured":"Winn, M. D. et al. Overview of the CCP4 suite and current developments. Acta. Crystallogr. D. Biol. Crystallogr. 67, 235\u2013242 (2011).","journal-title":"Acta. Crystallogr. D. Biol. Crystallogr."},{"key":"48253_CR46","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","volume":"596","author":"J Jumper","year":"2021","unstructured":"Jumper, J. et al. Highly accurate protein structure prediction with AlphaFold. Nature 596, 583\u2013589 (2021).","journal-title":"Nature"},{"key":"48253_CR47","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. D. Features and development of Coot. Acta Crystallogr. D. Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"48253_CR48","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D. Biol. Crystallogr. 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"48253_CR49","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1107\/S0021889892009944","volume":"26","author":"RA Laskowski","year":"1993","unstructured":"Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283\u2013291 (1993).","journal-title":"J. Appl. Crystallogr."},{"key":"48253_CR50","doi-asserted-by":"publisher","first-page":"477","DOI":"10.1007\/BF00228148","volume":"8","author":"RA Laskowski","year":"1996","unstructured":"Laskowski, R. A., Rulllman, J. A. C., MacArthur, M. W., Kaptein, R. & Thornton, J. M. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomole. NMR 8, 477\u2013486 (1996).","journal-title":"J. Biomole. NMR"},{"key":"48253_CR51","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D. Biol. Crystallogr. 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr. D. Biol. Crystallogr."},{"key":"48253_CR52","doi-asserted-by":"publisher","first-page":"W375","DOI":"10.1093\/nar\/gkm216","volume":"35","author":"IW Davis","year":"2007","unstructured":"Davis, I. W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35, W375\u2013W383 (2007).","journal-title":"Nucleic Acids Res"},{"key":"48253_CR53","doi-asserted-by":"publisher","first-page":"e4792","DOI":"10.1002\/pro.4792","volume":"32","author":"EC Meng","year":"2023","unstructured":"Meng, E. C. et al. UCSF ChimeraX: Tools for structure building and analysis. Protein Sci. 32, e4792 (2023).","journal-title":"Protein Sci."},{"key":"48253_CR54","unstructured":"Frisch, M. J. et al. Gaussian 16, Revision A.03. Gaussian, Inc., Wallingford CT (2016)."},{"key":"48253_CR55","doi-asserted-by":"publisher","first-page":"1193","DOI":"10.1128\/EC.00297-10","volume":"10","author":"BA Fox","year":"2011","unstructured":"Fox, B. A. et al. Type II Toxoplasma gondii KU80 Knockout Strains Enable Functional Analysis of Genes Required for Cyst Development and Latent Infection. Eukaryotic Cell 10, 1193\u20131206 (2011).","journal-title":"Eukaryotic Cell"},{"key":"48253_CR56","doi-asserted-by":"crossref","unstructured":"Tomita, T. et al. Toxoplasma gondii Matrix Antigen1 Is a Secreted Immunomodulatory Effector. mBio 12, 1\u201316 (2021).","DOI":"10.1128\/mBio.00603-21"}],"container-title":["Nature Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-48253-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-48253-w","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-48253-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,6]],"date-time":"2024-05-06T19:02:38Z","timestamp":1715022158000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41467-024-48253-w"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,5,6]]},"references-count":56,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["48253"],"URL":"https:\/\/doi.org\/10.1038\/s41467-024-48253-w","relation":{},"ISSN":["2041-1723"],"issn-type":[{"value":"2041-1723","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,5,6]]},"assertion":[{"value":"27 September 2023","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"23 April 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 May 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"3792"}}