ArticleJournal of the American Chemical Society2017
Designer α1,6-Fucosidase Mutants Enable Direct Core Fucosylation of Intact N-Glycopeptides and N-Glycoproteins.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- Fucoidans: a new frontier in brown seaweed research and biotechnology.Cell surface (Amsterdam, Netherlands) · 2026Review
- Transglycosylation Capabilities of Wild-Type α-l-Fucosidase iso1 from Paenibacillus thiaminolyticus and Its Engineered Mutants: Preparation of Fucosylated Oligosaccharides.Microbial biotechnology · 2026Article
- Selective fluorination of Fc glycans enhances antibody-mediated effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- FUT8 Regulates Cerebellar Neurogenesis and Development Through Maintaining the Level of Neural Cell Adhesion Molecule Cntn2.Molecular neurobiology · 2025Article
- Structure and function of microbial α-l-fucosidases: a mini review.Essays in biochemistry · 2023Review
- LC-MS/MS-PRM Quantification of IgG Glycoforms Using Stable Isotope Labeled IgG1 Fc Glycopeptide Standard.Journal of proteome research · 2023Article
- The Synthesis and Glycoside Formation of Polyfluorinated Carbohydrates.Chemical reviews · 2022Review
- Synthesis of glycopeptides and glycopeptide conjugates.Organic & biomolecular chemistry · 2022Review
- Sculpting therapeutic monoclonal antibody N-glycans using endoglycosidases.Current opinion in structural biology · 2022Review
- Cysteine-rich intestinal protein 1 enhances the progression of hepatocellular carcinoma via Ras signaling.The Kaohsiung journal of medical sciences · 2022Article
- Cell Free Remodeling of Glycosylation of Antibodies.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Comparative studies on the substrate specificity and defucosylation activity of three α-l-fucosidases using synthetic fucosylated glycopeptides and glycoproteins as substrates.Bioorganic & medicinal chemistry · 2021Article
- A facile chemoenzymatic synthesis of SARS-CoV-2 glycopeptides for probing glycosylation functions.Chemical communications (Cambridge, England) · 2021Article
- On the Use of Surface Plasmon Resonance Biosensing to Understand IgG-FcγR Interactions.International journal of molecular sciences · 2021Review
- Site-Selective Chemoenzymatic Modification on the Core Fucose of an Antibody Enhances Its Fcγ Receptor Affinity and ADCC Activity.Journal of the American Chemical Society · 2021Article
- Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation.Nature communications · 2020Article
- Functional exploration of the GH29 fucosidase family.Glycobiology · 2020Article
- A lectin-based glycomic approach identifies FUT8 as a driver of radioresistance in oesophageal squamous cell carcinoma.Cellular oncology (Dordrecht, Netherlands) · 2020Article
- α-L-Fucosidases and their applications for the production of fucosylated human milk oligosaccharides.Applied microbiology and biotechnology · 2020Review
- The Impact of Dietary Fucosylated Oligosaccharides and Glycoproteins of Human Milk on Infant Well-Being.Nutrients · 2020Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Core fucosylation of N-glycoproteins plays a crucial role in modulating the biological functions of glycoproteins. Yet, the synthesis of structurally well-defined, core-fucosylated glycoproteins remains a challenging task due to the complexity in multistep chemical synthesis or the inability of the biosynthetic α1,6-fucosyltransferase (FUT8) to directly fucosylate full-size mature N-glycans in a chemoenzymatic approach. We report in this paper the design and generation of potential α1,6-fucosynthase and fucoligase for direct core fucosylation of intact N-glycoproteins. We found that mutation at the nucleophilic residue (D200) did not provide a typical glycosynthase from this bacterial enzyme, but several mutants with mutation at the general acid/base residue E274 of the Lactobacillus casei α1,6-fucosidase, including E274A, E274S, and E274G, acted as efficient glycoligases that could fucosylate a wide variety of complex N-glycopeptides and intact glycoproteins by using α-fucosyl fluoride as a simple donor substrate. Studies on the substrate specificity revealed that the α1,6-fucosidase mutants could introduce an α1,6-fucose moiety specifically at the Asn-linked GlcNAc moiety not only to GlcNAc-peptide but also to high-mannose and complex-type N-glycans in the context of N-glycopeptides, N-glycoproteins, and intact antibodies. This discovery opens a new avenue to a wide variety of homogeneous, core-fucosylated N-glycopeptides and N-glycoproteins that are hitherto difficult to obtain for structural and functional studies.
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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.