ArticleProceedings of the National Academy of Sciences of the United States of America2024
A metabolic inhibitor blocks cellular fucosylation and enables production of afucosylated antibodies.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Exploiting human fucosyltransferase 8 allostery with a covalent inhibitor for core fucosylation suppression.Nature communications · 2026Article
- Structure, function, and implications of fucosyltransferases in health and disease.Nature communications · 2025Review
- C-6-Modified 2-F-Fucose Derivatives as Inhibitors of Fucosyltransferases.Chembiochem : a European journal of chemical biology · 2025Article
- Chemical Strategies to Custom-Modify α(1→3)-Fucosylated Glycan Motifs of the Human Glycocalyx.JACS Au · 2025Review
- Mutation of the GDP-Fucose Biosynthesis GeneInternational journal of molecular sciences · 2025Article
- Leveraging liquid biopsy to uncover resistance mechanisms and guide personalized immunotherapy.Translational oncology · 2025Review
- Kinetic Dissection of the Reaction of Human GDP-l-Fucose Synthase.ACS catalysis · 2025Article
- Realizing the promise of 'La Dolce Vita' via chemical biology: glycan-motif editing of sLeThe FEBS journal · 2025Review
- A gram-scale synthesis of β-L-carbafucose for engineering antibody glycans.Communications chemistry · 2025Article
- FUT8 Is a Critical Driver of Prostate Tumour Growth and Can Be Targeted Using Fucosylation Inhibitors.Cancer medicine · 2025Article
- ProteinMolecules (Basel, Switzerland) · 2025Review
- N-Acetylated Monosaccharides and Derived Glycan Structures Occurring in N- and O-Glycans During Prostate Cancer Development.Cancers · 2024Review
- 2,2-Difluoro Derivatives of Fucose Can Inhibit Cell Surface Fucosylation without Causing Slow Transfer to Acceptors.JACS Au · 2024Article
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Authors and funding
18 authors.
Funding
Abstract
The fucosylation of glycoproteins regulates diverse physiological processes. Inhibitors that can control cellular levels of protein fucosylation have consequently emerged as being of high interest. One area where inhibitors of fucosylation have gained significant attention is in the production of afucosylated antibodies, which exhibit superior antibody-dependent cell cytotoxicity as compared to their fucosylated counterparts. Here, we describe β-carbafucose, a fucose derivative in which the endocyclic ring oxygen is replaced by a methylene group, and show that it acts as a potent metabolic inhibitor within cells to antagonize protein fucosylation. β-carbafucose is assimilated by the fucose salvage pathway to form GDP-carbafucose which, due to its being unable to form the oxocarbenium ion-like transition states used by fucosyltransferases, is an incompetent substrate for these enzymes. β-carbafucose treatment of a CHO cell line used for high-level production of the therapeutic antibody Herceptin leads to dose-dependent reductions in core fucosylation without affecting cell growth or antibody production. Mass spectrometry analyses of the intact antibody and
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