Insertion of N-terminal hinge glycosylation enhances interactions of the Fc region of human IgG1 monomers with glycan-dependent receptors and blocks hemagglutination by the influenza virus
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In therapeutic applications in which the Fc of IgG is critically important, the receptor binding and functional properties of the Fc are lost after deglycosylation or removal of the unique Asn297 N-X-(T/S) sequon. A population of Fcs bearing sialylated glycans has been identified as contributing to this functionality, and high levels of sialylation also lead to longer serum retention times advantageous for therapy. The efficacy of sialylated Fc has generated an incentive to modify the unique N-linked glycosylation site at Asn297, either through chemical and enzymatic methods or by mutagenesis of the Fc, that disrupts the protein–Asn297 carbohydrate interface. In this study, we took an alternative approach by inserting or deleting N-linked attachment sites into the body of the Fc to generate a portfolio of mutants with tailored effector functions. For example, we describe mutants with enhanced binding to low-affinity inhibitory human Fcγ and glycan receptors that may be usefully incorporated into existing Ab engineering approaches to treat or vaccinate against disease. The IgG1 Fc fragments containing complex sialylated glycans attached to the N-terminal Asn221 sequon bound influenza virus hemagglutinin and disrupted influenza A–mediated agglutination of human erythrocytes.
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Some hypersialylated mutants bind influenza viruses with high affinity and inhibit influenza-mediated hemagglutination.
“Some of these hypersialylated mutants were also found to bind influenza viruses with high-affinity and inhibit influenza-mediated hemagglutination [121,122].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [121]
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Vrettou, C., Blundell, P. A., Gaunt, E. R., & Pleass, R. J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.06.511107 · Cited by 1 · see citing works
Self-citationWillinger, O., Granik, N., Goldberg, S., & Amit, R. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.28.610020
Li, Y., Xie, S., Chen, M., Li, H., Wang, Y., Fan, Y., An, K., Wu, Y., & Xiao, W. (2024) · Figshare · doi:10.6084/m9.figshare.26581706
- Authors
- Blundell, P. A., Lu, D., Wilkinson, M., Dell, A., Haslam, S., & Pleass, R. J.
- Affiliations
- Liverpool School of Tropical Medicine (GB)
- Imperial College London (GB)
- Corresponding author
- Wilkinson, Mark
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2019-03-01
- Volume
- 202
- Issue
- 5
- Pages
- 1595-1611
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- PMC
- PMC6379808
- OpenAlex
- W2912885282
- Cited by
- 11
- References
- 78
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2018: 1
- FWCI
- 0.83
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- The Journal of Immunology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- LSTM Online Archive (Liverpool School of Tropical Medicine) (acceptedVersion)
- Funders
- Wellcome Trust (109469/Z/15/Z, 109469, 097830/Z/11/Z, 208938/Z/17/Z)
- Medical Research Council (MC_PC_12017, MC_PC_16078)
- Biotechnology and Biological Sciences Research Council (BB/F008309/1)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
- Keywords
- IgG1 Fc, sialylated glycans, Fc gamma receptor, glycan receptors, influenza virus hemagglutinin, hemagglutination inhibition, antibody engineering, serum half-life
- MeSH terms
- Glycosylation, Hemagglutination, Humans, Immunoglobulin G, Immunoglobulin Fc Fragments, Mutation, Orthomyxoviridae, Polysaccharides, Receptors, IgG
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