By a News Reporter-Staff News Editor at Biotech Week -- New research on Enzymes and Coenzymes is the subject of a report. According to news originating from Burnaby, Canada, by NewsRx correspondents, research stated, "Mucopolysaccharidosis (MPS) I is a lysosomal storage disease caused by a deficiency of ?-L-iduronidase (IDUA) (EC 184.108.40.206); enzyme replacement therapy is the conventional treatment for this genetic disease. Arabidopsis cgl mutants are characterized by a deficiency of the activity of N-acetylglucosaminyl transferase I (EC 220.127.116.11), the first enzyme in the pathway of hybrid and complex N-glycan biosynthesis."
Our news journalists obtained a quote from the research from Simon Fraser University, "To develop a seed-based platform for the production of recombinant IDUA for potential treatment of MPS I, cgl mutant seeds were generated to express human IDUA at high yields and to avoid maturation of the N-linked glycans on the recombinant human enzyme. Enzyme kinetic data showed that cgl-IDUA has similar enzymatic properties to the commercial recombinant IDUA derived from cultured Chinese hamster ovary (CHO) cells (Aldurazyme™). The N-glycan profile showed that cgl-derived IDUA contained predominantly high-mannose-type N-glycans (94.5%), and the residual complex/hybrid N-glycan-containing enzyme was efficiently removed by an additional affinity chromatography step. Furthermore, purified cgl-IDUA was amenable to sequential in vitro processing by soluble recombinant forms of the two enzymes that mediate the addition of the mannose-6-phosphate (M6P) tag in mammalian cells-UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine (GlcNAc)-1-phosphotransferase-and GlcNAc-1-phosphodiester ?-N-acetylglucosaminidase (the 'uncovering enzyme')."
According to the news editors, the research concluded: "Arabidopsis 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 M6P, a recognition marker essential for efficient receptor-mediated uptake into lysosomes of human cells."
For more information on this research see: Characterization and downstream mannose phosphorylation of human recombinant ?-L-iduronidase produced in Arabidopsis complex glycan-deficient (cgl) seeds. Plant Biotechnology Journal, 2013;11(9):1034-43. Plant Biotechnology Journal can be contacted at: Blackwell Publishing Inc, 350 Main St, Malden, MA 02148, USA. (Wiley-Blackwell - www.wiley.com/; Plant Biotechnology Journal - onlinelibrary.wiley.com/journal/10.1111/(ISSN)1467-7652)
The news correspondents report that additional information may be obtained from X. He, Dept. of Biological Sciences, Simon Fraser University, Burnaby, BC, Canada. Additional authors for this research include O. Pierce, T. Haselhorst, M. von Itzstein, D. Kolarich, N.H. Packer, T.M. Gloster, D.J. Vocadlo, Y. Qian, D. Brooks and A.R Kermode (see also Enzymes and Coenzymes).
The publisher's contact information for the Plant Biotechnology Journal is: Blackwell Publishing Inc, 350 Main St, Malden, MA 02148, USA.
Keywords for this news article include: Canada, Burnaby, Therapy, Treatment, Iduronidase, British Columbia, Glycoside Hydrolases, Enzymes and Coenzymes, North and Central America.
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