{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T18:34:20Z","timestamp":1764700460050},"reference-count":41,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2013,7,31]],"date-time":"2013-07-31T00:00:00Z","timestamp":1375228800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Plant Biotechnology Journal"],"published-print":{"date-parts":[[2013,12]]},"abstract":"Summary<\/jats:title>Mucopolysaccharidosis (MPS<\/jats:styled-content>) I is a lysosomal storage disease caused by a deficiency of \u03b1\u2010L<\/jats:styled-content>\u2010iduronidase (IDUA<\/jats:styled-content>) (EC<\/jats:styled-content> 3.2.1.76); enzyme replacement therapy is the conventional treatment for this genetic disease. A<\/jats:styled-content>rabidopsis cgl<\/jats:italic> mutants are characterized by a deficiency of the activity of N<\/jats:styled-content><\/jats:italic>\u2010acetylglucosaminyl transferase I<\/jats:styled-content> (EC<\/jats:styled-content> 2.4.1.101), the first enzyme in the pathway of hybrid and complex N<\/jats:styled-content><\/jats:italic>\u2010glycan biosynthesis. To develop a seed\u2010based platform for the production of recombinant IDUA<\/jats:styled-content> for potential treatment of MPS I<\/jats:styled-content>, cgl<\/jats:italic> mutant seeds were generated to express human IDUA<\/jats:styled-content> at high yields and to avoid maturation of the N<\/jats:styled-content><\/jats:italic>\u2010linked glycans on the recombinant human enzyme. Enzyme kinetic data showed that cgl<\/jats:italic>\u2010IDUA<\/jats:styled-content> has similar enzymatic properties to the commercial recombinant IDUA<\/jats:styled-content> derived from cultured C<\/jats:styled-content>hinese hamster ovary (CHO<\/jats:styled-content>) cells (A<\/jats:styled-content>ldurazymeTM<\/jats:sup><\/jats:styled-content>). The N<\/jats:styled-content><\/jats:italic>\u2010glycan profile showed that cgl<\/jats:italic>\u2010derived IDUA<\/jats:styled-content> contained predominantly high\u2010mannose\u2010type N<\/jats:styled-content><\/jats:italic>\u2010glycans (94.5%), and the residual complex\/hybrid N<\/jats:styled-content><\/jats:italic>\u2010glycan\u2010containing enzyme was efficiently removed by an additional affinity chromatography step. Furthermore, purified cgl<\/jats:italic>\u2010IDUA<\/jats:styled-content> was amenable to sequential in vitro<\/jats:italic> processing by soluble recombinant forms of the two enzymes that mediate the addition of the mannose\u20106\u2010phosphate (M<\/jats:styled-content>6P<\/jats:styled-content>) tag in mammalian cells\u2014UDP<\/jats:styled-content>\u2010GlcNA<\/jats:styled-content>c:lysosomal enzyme N<\/jats:styled-content><\/jats:italic>\u2212acetylglucosamine (G<\/jats:styled-content>lcNA<\/jats:styled-content>c)\u22121\u2212phosphotransferase\u2014and GlcNA<\/jats:styled-content>c\u22121\u2212phosphodiester \u03b1\u2212N<\/jats:styled-content><\/jats:italic>\u2212acetylglucosaminidase (the \u2018uncovering enzyme\u2019). A<\/jats:styled-content>rabidopsis<\/jats:italic> seeds provide an alternative system for producing recombinant lysosomal enzymes for enzyme replacement therapy; the purified enzymes can be subjected to downstream processing to create the M<\/jats:styled-content>6P<\/jats:styled-content>, a recognition marker essential for efficient receptor\u2010mediated uptake into lysosomes of human cells.<\/jats:p><\/jats:sec>","DOI":"10.1111\/pbi.12096","type":"journal-article","created":{"date-parts":[[2013,7,31]],"date-time":"2013-07-31T08:20:25Z","timestamp":1375258825000},"page":"1034-1043","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":20,"title":["Characterization and downstream mannose phosphorylation of human recombinant \u03b1\u2010L<\/scp>\u2010iduronidase produced in A<\/scp>rabidopsis complex glycan\u2010deficient<\/i> (cgl<\/i>) seeds"],"prefix":"10.1111","volume":"11","author":[{"given":"Xu","family":"He","sequence":"first","affiliation":[{"name":"Department of Biological Sciences Simon Fraser University Burnaby BC Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Owen","family":"Pierce","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Simon Fraser University Burnaby BC Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thomas","family":"Haselhorst","sequence":"additional","affiliation":[{"name":"Institute for Glycomics Griffith University Southport Qld Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark","family":"von Itzstein","sequence":"additional","affiliation":[{"name":"Institute for Glycomics Griffith University Southport Qld Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel","family":"Kolarich","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biomolecular Sciences Macquarie University Sydney NSW Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicolle H.","family":"Packer","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Biomolecular Sciences Macquarie University Sydney NSW Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tracey M.","family":"Gloster","sequence":"additional","affiliation":[{"name":"Department of Chemistry Simon Fraser University Burnaby BC Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David J.","family":"Vocadlo","sequence":"additional","affiliation":[{"name":"Department of Chemistry Simon Fraser University Burnaby BC Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yi","family":"Qian","sequence":"additional","affiliation":[{"name":"Department of Internal Medicine Washington University School of Medicine St. Louis MO USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Doug","family":"Brooks","sequence":"additional","affiliation":[{"name":"Sansom Institute School of Pharmacy and Medical Sciences University of South Australia Adelaide SA Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Allison R.","family":"Kermode","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences Simon Fraser University Burnaby BC Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2013,7,31]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.271.49.31437"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1017\/S1462399408000550"},{"key":"e_1_2_6_4_1","doi-asserted-by":"crossref","first-page":"6326","DOI":"10.1016\/S0021-9258(19)84566-0","article-title":"Phosphorylation of the oligosaccharide of uteroferrin by UDP\u2010GlcNAc:glycoprotein N\u2010acetylglucosamine\u20101\u2010phosphotransferases from rat liver, Acanthamoeba castellani, and Dictyostelium discoideum requires alpha 1, 2\u2010linked mannose residues","volume":"261","author":"Couso R.","year":"1986","journal-title":"J. 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