ArticleNature communications2019
The glycosylation design space for recombinant lysosomal replacement enzymes produced in CHO cells.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 63 citations in OpenAlex.
- Quantitative and Comparative Assessment of Recombinant Human β-Glucocerebrosidase Uptake Bioactivity Using a Stable hMMR-Expressing CHO Cell Model.Molecules (Basel, Switzerland) · 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
- Targeted nanoliposomes to improve enzyme replacement therapy of Fabry disease.Science advances · 2024Article
- Mammalian cell-based production of glycans, glycopeptides and glycomodules.Nature communications · 2024Article
- Expression of influenza A virus glycan receptor candidates in mallard, chicken, and tufted duck.Glycobiology · 2024Article
- Pegunigalsidase alfa: a novel, pegylated recombinant alpha-galactosidase enzyme for the treatment of Fabry disease.Frontiers in genetics · 2024Review
- Glycosylation shapes the efficacy and safety of diverse protein, gene and cell therapies.Biotechnology advances · 2023Review
- Development of a Biosimilar of Agalsidase Beta for the Treatment of Fabry Disease: Preclinical Evaluation.Drugs in R&D · 2023Article
- CRISPR Technologies in Chinese Hamster Ovary Cell Line Engineering.International journal of molecular sciences · 2023Review
- Optimizing human α-galactosidase for treatment of Fabry disease.Scientific reports · 2023Article
- Identification of global inhibitors of cellular glycosylation.Nature communications · 2023Article
- A universal GlycoDesign for lysosomal replacement enzymes to improve circulation time and biodistribution.Frontiers in bioengineering and biotechnology · 2023Article
- An etanercept O-glycovariant with enhanced potency.Molecular therapy. Methods & clinical development · 2022Article
- N-terminome analyses underscore the prevalence of SPPL3-mediated intramembrane proteolysis among Golgi-resident enzymes and its role in Golgi enzyme secretion.Cellular and molecular life sciences : CMLS · 2022Article
- New Opportunities in Glycan Engineering for Therapeutic Proteins.Antibodies (Basel, Switzerland) · 2022Review
- Role ofFrontiers in immunology · 2022Article
- Therapeutic Approaches in Lysosomal Storage Diseases.Biomolecules · 2021Review
- Chemoenzymatic glycan-selective remodeling of a therapeutic lysosomal enzyme with high-affinity M6P-glycan ligands. Enzyme substrate specificity is the name of the game.Chemical science · 2021Article
- Migalastat Tissue Distribution: Extrapolation From Mice to Humans Using Pharmacokinetic Modeling and Comparison With Agalsidase Beta Tissue Distribution in Mice.Clinical pharmacology in drug development · 2021Article
- FUT8-Directed Core Fucosylation of N-glycans Is Regulated by the Glycan Structure and Protein Environment.ACS catalysis · 2021Article
Corrections and comments
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Authors and funding
18 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysosomal replacement enzymes are essential therapeutic options for rare congenital lysosomal enzyme deficiencies, but enzymes in clinical use are only partially effective due to short circulatory half-life and inefficient biodistribution. Replacement enzymes are primarily taken up by cell surface glycan receptors, and glycan structures influence uptake, biodistribution, and circulation time. It has not been possible to design and systematically study effects of different glycan features. Here we present a comprehensive gene engineering screen in Chinese hamster ovary cells that enables production of lysosomal enzymes with N-glycans custom designed to affect key glycan features guiding cellular uptake and circulation. We demonstrate distinct circulation time and organ distribution of selected glycoforms of α-galactosidase A in a Fabry disease mouse model, and find that an α2-3 sialylated glycoform designed to eliminate uptake by the mannose 6-phosphate and mannose receptors exhibits improved circulation time and targeting to hard-to-reach organs such as heart. The developed design matrix and engineered CHO cell lines enables systematic studies towards improving enzyme replacement therapeutics.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.