{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T21:58:28Z","timestamp":1781128708702,"version":"3.54.1"},"reference-count":57,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,10,4]],"date-time":"2024-10-04T00:00:00Z","timestamp":1728000000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2024,10,4]],"date-time":"2024-10-04T00:00:00Z","timestamp":1728000000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-024-73778-x","type":"journal-article","created":{"date-parts":[[2024,10,4]],"date-time":"2024-10-04T08:02:11Z","timestamp":1728028931000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Production of active human iduronate-2-sulfatase (IDS) enzyme in Nicotiana benthamiana"],"prefix":"10.1038","volume":"14","author":[{"given":"Md Hasif","family":"Sinha","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tahrin","family":"Mehtab","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mehrnaz","family":"Entesari","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong Hanh","family":"Nguyen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Areum","family":"Yun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Inhwan","family":"Hwang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,10,4]]},"reference":[{"key":"73778_CR1","doi-asserted-by":"publisher","first-page":"100692","DOI":"10.1016\/j.ymgmr.2020.100692","volume":"25","author":"Y Fukuhara","year":"2020","unstructured":"Fukuhara, Y. et al. A cDNA analysis disclosed the discordance of genotype-phenotype correlation in a patient with attenuated MPS II and a 76-base deletion in the gene for iduronate-2-sulfatase. Mol. Genet. Metab. Rep.25, 100692. https:\/\/doi.org\/10.1016\/j.ymgmr.2020.100692 (2020).","journal-title":"Mol. Genet. Metab. Rep."},{"key":"73778_CR2","doi-asserted-by":"publisher","first-page":"2467","DOI":"10.2147\/dddt.S139601","volume":"11","author":"DA Whiteman","year":"2017","unstructured":"Whiteman, D. A. & Kimura, A. Development of idursulfase therapy for mucopolysaccharidosis type II (Hunter syndrome): the past, the present and the future. Drug Des. Devel Ther.11, 2467\u20132480. https:\/\/doi.org\/10.2147\/dddt.S139601 (2017).","journal-title":"Drug Des. Devel Ther."},{"key":"73778_CR3","doi-asserted-by":"publisher","first-page":"100563","DOI":"10.1016\/j.ymgmr.2019.100563","volume":"22","author":"M Stapleton","year":"2020","unstructured":"Stapleton, M. et al. Newborn screening for mucopolysaccharidoses: measurement of glycosaminoglycans by LC-MS\/MS. Mol. Genet. Metab. Rep.22, 100563. https:\/\/doi.org\/10.1016\/j.ymgmr.2019.100563 (2020).","journal-title":"Mol. Genet. Metab. Rep."},{"key":"73778_CR4","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1002\/bab.1660","volume":"65","author":"N Pimentel","year":"2018","unstructured":"Pimentel, N. et al. Production and characterization of a human lysosomal recombinant iduronate-2\u2010sulfatase produced in Pichia pastoris. Biotechnol. Appl. Biochem.65, 655\u2013664 (2018).","journal-title":"Biotechnol. Appl. Biochem."},{"key":"73778_CR5","doi-asserted-by":"publisher","first-page":"1110","DOI":"10.3390\/biom10081110","volume":"10","author":"Pinto","year":"2020","unstructured":"Pinto et al. Precision medicine for lysosomal disorders. Biomolecules. 10, 1110 (2020).","journal-title":"Biomolecules"},{"key":"73778_CR6","doi-asserted-by":"crossref","unstructured":"Tomatsu, S. et al. Impact of enzyme replacement therapy and hematopoietic stem cell transplantation in patients with Morquio A syndrome. Drug Des. Dev. Therapy, 1937\u20131953 (2015).","DOI":"10.2147\/DDDT.S68562"},{"key":"73778_CR7","doi-asserted-by":"publisher","first-page":"1187","DOI":"10.1038\/gim.2017.30","volume":"19","author":"LA Bradley","year":"2017","unstructured":"Bradley, L. A., Haddow, H. R. & Palomaki, G. E. Treatment of mucopolysaccharidosis type II (Hunter syndrome): results from a systematic evidence review. Genet. Med.19, 1187\u20131201 (2017).","journal-title":"Genet. Med."},{"key":"73778_CR8","doi-asserted-by":"publisher","first-page":"79","DOI":"10.5582\/irdr.2014.01013","volume":"3","author":"SY Cho","year":"2014","unstructured":"Cho, S. Y., Sohn, Y. B. & Jin, D. K. An overview of Korean patients with mucopolysaccharidosis and collaboration through the Asia Pacific MPS network. Intractable Rare Dis. Res.3, 79\u201386 (2014).","journal-title":"Intractable Rare Dis. Res."},{"key":"73778_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/1475-2859-8-17","volume":"8","author":"N Ferrer-Miralles","year":"2009","unstructured":"Ferrer-Miralles, N., Domingo-Esp\u00edn, J., Corchero, J. L., V\u00e1zquez, E. & Villaverde, A. Microbial factories for recombinant pharmaceuticals. Microb. Cell. Fact.8, 1\u20138 (2009).","journal-title":"Microb. Cell. Fact."},{"key":"73778_CR10","doi-asserted-by":"publisher","first-page":"153359","DOI":"10.1016\/j.jplph.2020.153359","volume":"258","author":"S Schillberg","year":"2021","unstructured":"Schillberg, S. & Finnern, R. Plant molecular farming for the production of valuable proteins\u2013critical evaluation of achievements and future challenges. J. Plant. Physiol.258, 153359 (2021).","journal-title":"J. Plant. Physiol."},{"key":"73778_CR11","doi-asserted-by":"publisher","first-page":"1199","DOI":"10.1111\/pbi.12428","volume":"13","author":"Y Tekoah","year":"2015","unstructured":"Tekoah, Y. et al. Large-scale production of pharmaceutical proteins in plant cell culture\u2014the protalix experience. Plant. Biotechnol. J.13, 1199\u20131208 (2015).","journal-title":"Plant. Biotechnol. J."},{"key":"73778_CR12","doi-asserted-by":"publisher","first-page":"908","DOI":"10.1002\/jimd.12228","volume":"43","author":"SJ van der Veen","year":"2020","unstructured":"van der Veen, S. J., Hollak, C. E., van Kuilenburg, A. B. & Langeveld, M. Developments in the treatment of fabry disease. J. Inherit. Metab. Dis.43, 908\u2013921 (2020).","journal-title":"J. Inherit. Metab. Dis."},{"key":"73778_CR13","doi-asserted-by":"crossref","unstructured":"Wani, K. I. & Aftab, T. Plant Molecular Farming: Applications and new Directions (Springer Nature, 2022).","DOI":"10.1007\/978-3-031-12794-6"},{"key":"73778_CR14","doi-asserted-by":"publisher","first-page":"922694","DOI":"10.3389\/fpls.2022.922694","volume":"13","author":"AP Soni","year":"2022","unstructured":"Soni, A. P., Lee, J., Shin, K., Koiwa, H. & Hwang, I. Production of recombinant active human TGF\u03b21 in nicotiana Benthamiana. Front. Plant. Sci.13, 922694 (2022).","journal-title":"Front. Plant. Sci."},{"key":"73778_CR15","doi-asserted-by":"publisher","first-page":"405","DOI":"10.1146\/annurev-phyto-080417-050141","volume":"56","author":"J Bally","year":"2018","unstructured":"Bally, J. et al. The rise and rise of Nicotiana benthamiana: a plant for all reasons. Ann. Rev. Phytopathol.56, 405\u2013426 (2018).","journal-title":"Ann. Rev. Phytopathol."},{"key":"73778_CR16","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1046\/j.1365-313X.1992.t01-41-00999.x","volume":"2","author":"CI Wandelt","year":"1992","unstructured":"Wandelt, C. I. et al. Vicilin with carboxy-terminal KDEL is retained in the endoplasmic reticulum and accumulates to high levels in the leaves of transgenic plants. Plant. J.2, 181\u2013192. https:\/\/doi.org\/10.1046\/j.1365-313X.1992.t01-41-00999.x (1992).","journal-title":"Plant. J."},{"key":"73778_CR17","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1110\/ps.22102","volume":"11","author":"M Hammarstr\u00f6m","year":"2002","unstructured":"Hammarstr\u00f6m, M., Hellgren, N., van den Berg, S., Berglund, H. & H\u00e4rd, T. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci.11, 313\u2013321. https:\/\/doi.org\/10.1110\/ps.22102 (2002).","journal-title":"Protein Sci."},{"key":"73778_CR18","doi-asserted-by":"publisher","first-page":"813","DOI":"10.1080\/13102818.2016.1166984","volume":"30","author":"XWXFDD Xueming Zheng","year":"2016","unstructured":"Xueming Zheng, X. W. X. F. D. D. & Feihu, W. Expression and purification of human epidermal growth factor (hEGF) fused with GB1. Biotechnol. Biotechnol. Equip.30, 813\u2013818. https:\/\/doi.org\/10.1080\/13102818.2016.1166984 (2016).","journal-title":"Biotechnol. Biotechnol. Equip."},{"key":"73778_CR19","doi-asserted-by":"publisher","first-page":"878677","DOI":"10.3389\/fpls.2022.878677","volume":"13","author":"SJ Song","year":"2022","unstructured":"Song, S. J., Diao, H. P., Moon, B., Yun, A. & Hwang, I. The B1 domain of streptococcal protein G serves as a multi-functional tag for recombinant protein production in plants. Front. Plant. Sci.13, 878677 (2022).","journal-title":"Front. Plant. Sci."},{"key":"73778_CR20","doi-asserted-by":"publisher","first-page":"4612","DOI":"10.1038\/s41598-018-22860-2","volume":"8","author":"H Kang","year":"2018","unstructured":"Kang, H., Park, Y., Lee, Y., Yoo, Y. J. & Hwang, I. Fusion of a highly N-glycosylated polypeptide increases the expression of ER-localized proteins in plants. Sci. Rep.8, 4612 (2018).","journal-title":"Sci. Rep."},{"key":"73778_CR21","doi-asserted-by":"publisher","first-page":"314","DOI":"10.1016\/j.pep.2008.02.015","volume":"59","author":"SH Shahravan","year":"2008","unstructured":"Shahravan, S. H., Qu, X., Chan, I. S. & Shin, J. A. Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag. Protein Express Purif.59, 314\u2013319 (2008).","journal-title":"Protein Express Purif."},{"key":"73778_CR22","doi-asserted-by":"publisher","first-page":"1094","DOI":"10.1111\/pbi.13040","volume":"17","author":"MR Islam","year":"2019","unstructured":"Islam, M. R. et al. Cost-effective production of tag\u2010less recombinant protein in Nicotiana Benthamiana. Plant. Biotechnol. J.17, 1094\u20131105 (2019).","journal-title":"Plant. Biotechnol. J."},{"key":"73778_CR23","doi-asserted-by":"publisher","first-page":"2298","DOI":"10.1111\/pbi.13908","volume":"20","author":"SJ Song","year":"2022","unstructured":"Song, S. J. et al. SARS-CoV-2 spike trimer vaccine expressed in Nicotiana benthamiana adjuvanted with Alum elicits protective immune responses in mice. Plant. Biotechnol. J.20, 2298\u20132312. https:\/\/doi.org\/10.1111\/pbi.13908 (2022).","journal-title":"Plant. Biotechnol. J."},{"key":"73778_CR24","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1093\/nar\/gkt864","volume":"42","author":"Y Kim","year":"2014","unstructured":"Kim, Y. et al. The immediate upstream region of the 5\u2019-UTR from the AUG start codon has a pronounced effect on the translational efficiency in Arabidopsis thaliana. Nucleic Acids Res.42, 485\u2013498. https:\/\/doi.org\/10.1093\/nar\/gkt864 (2014).","journal-title":"Nucleic Acids Res."},{"key":"73778_CR25","doi-asserted-by":"publisher","first-page":"1138089","DOI":"10.3389\/fpls.2023.1138089","volume":"14","author":"A Yun","year":"2023","unstructured":"Yun, A., Kang, J., Lee, J., Song, S. J. & Hwang, I. Design of an artificial transcriptional system for production of high levels of recombinant proteins in tobacco (Nicotiana Benthamiana). Front. Plant. Sci.14, 1138089 (2023).","journal-title":"Front. Plant. Sci."},{"key":"73778_CR26","doi-asserted-by":"publisher","first-page":"485","DOI":"10.1093\/nar\/gkt864","volume":"42","author":"Y Kim","year":"2014","unstructured":"Kim, Y. et al. The immediate upstream region of the 5\u2032-UTR from the AUG start codon has a pronounced effect on the translational efficiency in Arabidopsis thaliana. Nucleic Acids Res.42, 485\u2013498 (2014).","journal-title":"Nucleic Acids Res."},{"key":"73778_CR27","doi-asserted-by":"publisher","first-page":"511","DOI":"10.1128\/JVI.77.1.511-522.2003","volume":"77","author":"F Qu","year":"2003","unstructured":"Qu, F., Ren, T. & Morris, T. J. The coat protein of turnip crinkle virus suppresses posttranscriptional gene silencing at an early initiation step. J. Virol.77, 511\u2013522 (2003).","journal-title":"J. Virol."},{"key":"73778_CR28","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1111\/j.1399-3054.2009.01223.x","volume":"136","author":"XY Jia","year":"2009","unstructured":"Jia, X. Y., He, L. H., Jing, R. L. & Li, R. Z. Calreticulin: conserved protein and diverse functions in plants. Physiol. Plant.136, 127\u2013138 (2009).","journal-title":"Physiol. Plant."},{"key":"73778_CR29","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1016\/S0042-6822(02)00018-1","volume":"306","author":"CL Thomas","year":"2003","unstructured":"Thomas, C. L., Leh, V., Lederer, C. & Maule, A. J. Turnip crinkle virus coat protein mediates suppression of RNA silencing in nicotiana Benthamiana. Virology. 306, 33\u201341. https:\/\/doi.org\/10.1016\/S0042-6822(02)00018-1 (2003).","journal-title":"Virology"},{"key":"73778_CR30","doi-asserted-by":"publisher","first-page":"2109","DOI":"10.1111\/pbi.13369","volume":"18","author":"E Margolin","year":"2020","unstructured":"Margolin, E. et al. Co-expression of human calreticulin significantly improves the production of HIV gp140 and other viral glycoproteins in plants. Plant. Biotechnol. J.18, 2109\u20132117 (2020).","journal-title":"Plant. Biotechnol. J."},{"key":"73778_CR31","doi-asserted-by":"publisher","first-page":"435","DOI":"10.1016\/S0092-8674(03)00347-7","volume":"113","author":"T Dierks","year":"2003","unstructured":"Dierks, T. et al. Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C\u03b1-formylglycine generating enzyme. Cell. 113, 435\u2013444 (2003).","journal-title":"Cell"},{"key":"73778_CR32","doi-asserted-by":"publisher","first-page":"30019","DOI":"10.1074\/jbc.M113.499541","volume":"288","author":"EM Wiegmann","year":"2013","unstructured":"Wiegmann, E. M. et al. Arylsulfatase K, a novel lysosomal sulfatase. J. Biol. Chem.288, 30019\u201330028 (2013).","journal-title":"J. Biol. Chem."},{"key":"73778_CR33","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1016\/j.gim.2021.12.013","volume":"24","author":"ET Strovel","year":"2022","unstructured":"Strovel, E. T., Cusmano-Ozog, K., Wood, T., Yu, C. & Committee, A. L. Q. A. Measurement of lysosomal enzyme activities: a technical standard of the American College of medical genetics and genomics (ACMG). Genet. Med.24, 769\u2013783 (2022).","journal-title":"Genet. Med."},{"key":"73778_CR34","doi-asserted-by":"publisher","first-page":"29329","DOI":"10.1038\/srep29329","volume":"6","author":"A Rodr\u00edguez-L\u00f3pez","year":"2016","unstructured":"Rodr\u00edguez-L\u00f3pez, A. et al. Recombinant human N-acetylgalactosamine-6-sulfate sulfatase (GALNS) produced in the methylotrophic yeast Pichia pastoris. Sci. Rep.6, 29329 (2016).","journal-title":"Sci. Rep."},{"key":"73778_CR35","doi-asserted-by":"publisher","first-page":"36","DOI":"10.1016\/j.ymgmr.2017.12.001","volume":"14","author":"R Mashima","year":"2018","unstructured":"Mashima, R., Ohira, M., Okuyama, T. & Tatsumi, A. Quantification of the enzyme activities of iduronate-2-sulfatase, N-acetylgalactosamine-6-sulfatase and N-acetylgalactosamine-4-sulfatase using liquid chromatography-tandem mass spectrometry. Mol. Genet. Metab. Rep.14, 36\u201340. https:\/\/doi.org\/10.1016\/j.ymgmr.2017.12.001 (2018).","journal-title":"Mol. Genet. Metab. Rep."},{"key":"73778_CR36","doi-asserted-by":"publisher","first-page":"563721","DOI":"10.3389\/fpls.2020.563721","volume":"11","author":"MA Razzak","year":"2020","unstructured":"Razzak, M. A., Lee, D. W., Lee, J. & Hwang, I. Overexpression and purification of Gracilariopsis Chorda carbonic anhydrase (GcCA\u03b13) in Nicotiana Benthamiana, and its immobilization and use in CO2 hydration reactions. Front. Plant. Sci.11, 563721 (2020).","journal-title":"Front. Plant. Sci."},{"key":"73778_CR37","doi-asserted-by":"publisher","first-page":"367","DOI":"10.4161\/hv.7.3.14303","volume":"7","author":"J Peters","year":"2011","unstructured":"Peters, J. & Stoger, E. Transgenic crops for the production of recombinant vaccines and anti-microbial antibodies. Hum. Vacc. 7, 367\u2013374 (2011).","journal-title":"Hum. Vacc"},{"key":"73778_CR38","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1016\/j.copbio.2007.03.002","volume":"18","author":"Y Gleba","year":"2007","unstructured":"Gleba, Y., Klimyuk, V. & Marillonnet, S. Viral vectors for the expression of proteins in plants. Curr. Opin. Biotechnol.18, 134\u2013141 (2007).","journal-title":"Curr. Opin. Biotechnol."},{"key":"73778_CR39","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.pep.2006.06.024","volume":"51","author":"W Peti","year":"2007","unstructured":"Peti, W. & Page, R. Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Express Purif.51, 1\u201310 (2007).","journal-title":"Protein Express Purif."},{"key":"73778_CR40","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1016\/j.pep.2007.10.018","volume":"57","author":"K Sugase","year":"2008","unstructured":"Sugase, K., Landes, M. A., Wright, P. E. & Martinez-Yamout, M. Overexpression of post-translationally modified peptides in Escherichia coli by co-expression with modifying enzymes. Protein Express Purif.57, 108\u2013115 (2008).","journal-title":"Protein Express Purif."},{"key":"73778_CR41","doi-asserted-by":"publisher","first-page":"331","DOI":"10.4161\/hv.7.3.14262","volume":"7","author":"Q Chen","year":"2011","unstructured":"Chen, Q., He, J., Phoolcharoen, W. & Mason, H. S. Geminiviral vectors based on bean yellow dwarf virus for production of vaccine antigens and monoclonal antibodies in plants. Hum. Vaccines.  7, 331\u2013338 (2011).","journal-title":"Hum. Vaccines"},{"key":"73778_CR42","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1093\/jxb\/erx262","volume":"69","author":"X Wang","year":"2018","unstructured":"Wang, X., Chung, K. P., Lin, W. & Jiang, L. Protein secretion in plants: conventional and unconventional pathways and new techniques. J. Exp. Bot.69, 21\u201337 (2018).","journal-title":"J. Exp. Bot."},{"key":"73778_CR43","doi-asserted-by":"publisher","first-page":"110","DOI":"10.1016\/j.pep.2015.12.018","volume":"120","author":"E \u0141ojewska","year":"2016","unstructured":"\u0141ojewska, E., Kowalczyk, T., Olejniczak, S. & Sakowicz, T. Extraction and purification methods in downstream processing of plant-based recombinant proteins. Protein Express Purif.120, 110\u2013117 (2016).","journal-title":"Protein Express Purif."},{"key":"73778_CR44","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1016\/S1046-5928(02)00012-8","volume":"25","author":"LD Yuan","year":"2002","unstructured":"Yuan, L. D. & Hua, Z. C. Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli. Protein Express Purif.25, 300\u2013304 (2002).","journal-title":"Protein Express Purif."},{"key":"73778_CR45","doi-asserted-by":"publisher","first-page":"5","DOI":"10.2225\/vol13-issue3-fulltext-8","volume":"13","author":"RA Poutou-Pi\u00f1ales","year":"2010","unstructured":"Poutou-Pi\u00f1ales, R. A. et al. Human sulfatase transiently and functionally active expressed in E. Coli K12. Electron. J. Biotechnol.13, 5\u20136 (2010).","journal-title":"Electron. J. Biotechnol."},{"key":"73778_CR46","doi-asserted-by":"publisher","first-page":"25560","DOI":"10.1074\/jbc.273.40.25560","volume":"273","author":"T Dierks","year":"1998","unstructured":"Dierks, T. et al. Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine. J. Biol. Chem.273, 25560\u201325564 (1998).","journal-title":"J. Biol. Chem."},{"key":"73778_CR47","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1016\/j.cell.2005.03.001","volume":"121","author":"T Dierks","year":"2005","unstructured":"Dierks, T. et al. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. Cell. 121, 541\u2013552 (2005).","journal-title":"Cell"},{"key":"73778_CR48","doi-asserted-by":"publisher","first-page":"6096","DOI":"10.1074\/jbc.273.11.6096","volume":"273","author":"M Recksiek","year":"1998","unstructured":"Recksiek, M., Selmer, T., Dierks, T., Schmidt, B. & von Figura, K. Sulfatases, trapping of the sulfated enzyme intermediate by substituting the active site formylglycine. J. Biol. Chem.273, 6096\u20136103 (1998).","journal-title":"J. Biol. Chem."},{"key":"73778_CR49","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ymgme.2014.02.011","volume":"112","author":"GA Grabowski","year":"2014","unstructured":"Grabowski, G. A., Golembo, M. & Shaaltiel, Y. Taliglucerase alfa: an enzyme replacement therapy using plant cell expression technology. Mol. Genet. Metab.112, 1\u20138. https:\/\/doi.org\/10.1016\/j.ymgme.2014.02.011 (2014).","journal-title":"Mol. Genet. Metab."},{"key":"73778_CR50","doi-asserted-by":"publisher","first-page":"1505","DOI":"10.1111\/jipb.13141","volume":"63","author":"SJ Song","year":"2021","unstructured":"Song, S. J. et al. Plant-based, adjuvant\u2010free, potent multivalent vaccines for avian influenza virus via Lactococcus surface display. J. Integr. Plant. Biol.63, 1505\u20131520 (2021).","journal-title":"J. Integr. Plant. Biol."},{"key":"73778_CR51","doi-asserted-by":"crossref","unstructured":"Shamloul, M., Trusa, J., Mett, V. & Yusibov, V. Optimization and utilization of Agrobacterium-mediated transient protein production in Nicotiana. JoVE, e51204 (2014).","DOI":"10.3791\/51204"},{"key":"73778_CR52","doi-asserted-by":"publisher","first-page":"297","DOI":"10.5511\/plantbiotechnology.21.0610a","volume":"38","author":"S Nosaki","year":"2021","unstructured":"Nosaki, S., Hoshikawa, K., Ezura, H. & Miura, K. Transient protein expression systems in plants and their applications. Plant. Biotechnol.38, 297\u2013304 (2021).","journal-title":"Plant. Biotechnol."},{"key":"73778_CR53","doi-asserted-by":"publisher","first-page":"289","DOI":"10.18388\/abp.2006_3341","volume":"53","author":"M Wydro","year":"2006","unstructured":"Wydro, M., Kozubek, E. & Lehmann, P. Optimization of transient Agrobacterium-mediated gene expression system in leaves of Nicotiana Benthamiana. Acta Biochim. Pol.53, 289\u2013298 (2006).","journal-title":"Acta Biochim. Pol."},{"key":"73778_CR54","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/s12870-021-02833-w","volume":"21","author":"L Zheng","year":"2021","unstructured":"Zheng, L. et al. An improved and efficient method of Agrobacterium syringe infiltration for transient transformation and its application in the elucidation of gene function in poplar. BMC Plant. Biol.21, 1\u201319 (2021).","journal-title":"BMC Plant. Biol."},{"key":"73778_CR55","doi-asserted-by":"crossref","unstructured":"Leuzinger, K. et al. Efficient agroinfiltration of plants for high-level transient expression of recombinant proteins. JoVE, e50521 (2013).","DOI":"10.3791\/50521-v"},{"key":"73778_CR56","doi-asserted-by":"publisher","DOI":"10.4172\/atbm.1000103","author":"Q Chen","year":"2013","unstructured":"Chen, Q. et al. Agroinfiltration as an effective and scalable strategy of gene delivery for production of pharmaceutical proteins. Adv. Tech. Biol. Med.https:\/\/doi.org\/10.4172\/atbm.1000103 (2013).","journal-title":"Adv. Tech. Biol. Med."},{"key":"73778_CR57","doi-asserted-by":"publisher","first-page":"769","DOI":"10.1016\/j.gim.2021.12.013","volume":"24","author":"ET Strovel","year":"2022","unstructured":"Strovel, E. T., Cusmano-Ozog, K., Wood, T. & Yu, C. Measurement of lysosomal enzyme activities: A technical standard of the American College of Medical Genetics and Genomics (ACMG). Genet. Medi. 24, 769\u2013783. https:\/\/doi.org\/10.1016\/j.gim.2021.12.013 (2022).","journal-title":"Genet. Medi"}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-73778-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-73778-x","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-73778-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,10,4]],"date-time":"2024-10-04T08:04:34Z","timestamp":1728029074000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-024-73778-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,10,4]]},"references-count":57,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["73778"],"URL":"https:\/\/doi.org\/10.1038\/s41598-024-73778-x","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,10,4]]},"assertion":[{"value":"22 July 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"20 September 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"4 October 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"23066"}}