ArticleProceedings of the National Academy of Sciences of the United States of America2011
Site-specific enzymatic polysialylation of therapeutic proteins using bacterial enzymes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
37 citing papers in PubMed, 111 citations in OpenAlex.
- Polysialic Acid Synthesis on theACS omega · 2026Article
- Molecular Survival Strategies Against Kidney Filtration: Implications for Therapeutic Protein Engineering.Biophysica · 2026Article
- Advances and challenges in plant N-glycoengineering: when fucosylation matters.Frontiers in plant science · 2025Review
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- Site-specific immobilization of the endosialidase reveals QSOX2 is a novel polysialylated protein.Glycobiology · 2024Article
- Producing Biologics with Defined N-Glycosylation in Plants.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Chemical Approaches to Synthetic Drug Delivery Systems for Systemic Applications.Angewandte Chemie (International ed. in English) · 2022Review
- Carbohydrate-active enzymes (CAZymes) in the gut microbiome.Nature reviews. Microbiology · 2022Review
- Targeted SERPIN (TaSER): A dual-action antithrombotic agent that targets platelets for SERPIN delivery.Journal of thrombosis and haemostasis : JTH · 2022Article
- 7-Fluorosialyl Glycosides Are Hydrolysis Resistant but Readily Assembled by Sialyltransferases Providing Easy Access to More Metabolically Stable Glycoproteins.ACS central science · 2021Article
- Enzymatic Synthesis of Glycans and Glycoconjugates.Advances in biochemical engineering/biotechnology · 2021Review
- Injectables and Depots to Prolong Drug Action of Proteins and Peptides.Pharmaceutics · 2020Review
- Synthetic Glycobiology: Parts, Systems, and Applications.ACS synthetic biology · 2020Review
- Engineering the serpin αProtein science : a publication of the Protein Society · 2020Review
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- Molecular Conformations of Di-, Tri-, and Tetra-International journal of molecular sciences · 2019Article
- Improving designer glycan production inMetabolic engineering communications · 2019Article
- A cell-free biosynthesis platform for modular construction of protein glycosylation pathways.Nature communications · 2019Article
- Oligosaccharide Synthesis and Translational Innovation.Journal of the American Chemical Society · 2019Review
- The Interaction of the Gut Microbiota with the Mucus Barrier in Health and Disease in Human.Microorganisms · 2018Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The posttranslational modification of therapeutic proteins with terminal sialic acids is one means of improving their circulating half-life, thereby improving their efficiency. We have developed a two-step in vitro enzymatic modification of glycoproteins, which has previously only been achieved by chemical means [Gregoriadis G, Jain S, Papaioannou I, Laing P (2005) Int J Pharm 300:125-130). This two-step procedure uses the Campylobacter jejuni Cst-II α2,8-sialyltransferase to provide a primer on N-linked glycans, followed by polysialylation using the Neisseria meningitidis α2,8-polysialyltransferase. Here, we have demonstrated the ability of this system to modify three glycoproteins with varying N-linked glycan compositions: the human therapeutic proteins alpha-1-antitrypsin (A1AT) and factor IX, as well as bovine fetuin. The chain length of the polysialic acid addition was optimized by controlling reaction conditions. After demonstrating the ability of this system to modify a variety of proteins, the effect of polysialylation on the activity and serum half-life of A1AT was examined. The polysialylation of A1AT did not adversely affect its in vitro inhibition activity against human neutrophil elastase. The polysialylation of A1AT resulted in a significantly improved pharmacokinetic profile when the modified proteins were injected into CD-1 mice. Together, these results suggest that polysialylated A1AT may be useful for improved augmentation therapy for patients with a deficiency in this protein and that this modification may be applied to other therapeutic proteins.
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Registered trials
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.