ArticleFrontiers in bioengineering and biotechnology2023
A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution.
Article in Frontiers in bioengineering and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Glycoengineered Recombinant Alpha1-Antitrypsin Results in Comparable In Vitro and In Vivo Activities to Human Plasma-Derived Protein.Biotechnology and bioengineering · 2026Article
- Integrated Glyco-Analytical Strategy for Comprehensive Characterization of a Complex Therapeutic Glycoprotein: Fabrazyme.International journal of molecular sciences · 2026Article
- Compositional and topological determinants of a physiological Ashwell-Morell receptor ligand.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mammalian cell-based production of glycans, glycopeptides and glycomodules.Nature communications · 2024Article
- Genetics of glycosylation in mammalian development and disease.Nature reviews. Genetics · 2024Review
- Comparison of efficacy between subcutaneous and intravenous application of moss-aGal in the mouse model of Fabry disease.JIMD reports · 2023Article
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Authors and funding
18 authors.
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Abstract
Currently available enzyme replacement therapies for lysosomal storage diseases are limited in their effectiveness due in part to short circulation times and suboptimal biodistribution of the therapeutic enzymes. We previously engineered Chinese hamster ovary (CHO) cells to produce α-galactosidase A (GLA) with various N-glycan structures and demonstrated that elimination of mannose-6-phosphate (M6P) and conversion to homogeneous sialylated N-glycans prolonged circulation time and improved biodistribution of the enzyme following a single-dose infusion into Fabry mice. Here, we confirmed these findings using repeated infusions of the glycoengineered GLA into Fabry mice and further tested whether this glycoengineering approach, Long-Acting-GlycoDesign (LAGD), could be implemented on other lysosomal enzymes. LAGD-engineered CHO cells stably expressing a panel of lysosomal enzymes [aspartylglucosamine (AGA), beta-glucuronidase (GUSB), cathepsin D (CTSD), tripeptidyl peptidase (TPP1), alpha-glucosidase (GAA) or iduronate 2-sulfatase (IDS)] successfully converted all M6P-containing N-glycans to complex sialylated N-glycans. The resulting homogenous glycodesigns enabled glycoprotein profiling by native mass spectrometry. Notably, LAGD extended the plasma half-life of all three enzymes tested (GLA, GUSB, AGA) in wildtype mice. LAGD may be widely applicable to lysosomal replacement enzymes to improve their circulatory stability and therapeutic efficacy.
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