Engineering the fragment crystallizable (Fc) region of human IgG1 multimers and monomers to fine-tune interactions with sialic acid-dependent receptors
Open accessAbstract
Multimeric fragment crystallizable (Fc) regions and Fc-fusion proteins are actively being explored as biomimetic replacements for IVIG therapy, which is deployed to manage many diseases and conditions but is expensive and not always efficient. The Fc region of human IgG1 (IgG1-Fc) can be engineered into multimeric structures (hexa-Fcs) that bind their cognate receptors with high avidity. The critical influence of the unique N -linked glycan attached at Asn-297 on the structure and function of IgG1-Fc is well documented; however, whether the N -linked glycan has a similarly critical role in multimeric, avidly binding Fcs, is unknown. Hexa-Fc contains two N -linked sites at Asn-77 (equivalent to Asn-297 in the Fc of IgG1) and Asn-236 (equivalent to Asn-563 in the tail piece of IgM). We report here that glycosylation at Asn-297 is critical for interactions with Fc receptors and complement and that glycosylation at Asn-563 is essential for controlling multimerization. We also found that introduction of an additional fully occupied N -linked glycosylation site at the N terminus at position 1 (equivalent to Asp-221 in the Fc of IgG1) dramatically enhances overall sialic acid content of the Fc multimers. Furthermore, replacement of Cys-575 in the IgM tail piece of multimers resulted in monomers with enhanced sialic acid content and differential receptor-binding profiles. Thus insertion of additional N -linked glycans into either the hinge or tail piece of monomers or multimers leads to molecules with enhanced sialylation that may be suitable for managing inflammation or blocking pathogen invasion.
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Insertion of a third N-glycosylation site at the N-terminus generated highly branched and hypersialylated glycans, which are mostly absent at the Asn297 site.
“The insertion of a third N-glycosylation site at the N-terminus generated highly branched and hypersialylated glycans, which are mostly absent at the Asn297 site and when combined with further mutation of Cys residues, was able to generate a range of monomers and multimers that have tailored interactions with sialic acid-dependent receptors [120].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [120]
Combining insertion of a third N-glycosylation site at the N-terminus with further mutation of Cys residues generated a range of monomers and multimers with tailored interactions with sialic acid-dependent receptors.
“The insertion of a third N-glycosylation site at the N-terminus generated highly branched and hypersialylated glycans, which are mostly absent at the Asn297 site and when combined with further mutation of Cys residues, was able to generate a range of monomers and multimers that have tailored interactions with sialic acid-dependent receptors [120].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [120]
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“The parental plasmids used for these new PCR reactions have been described previously (30).”
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Fc and tailpiece determinants of IgM tailpiece-mediated IgG hexamerisationPreprint
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- Authors
- Blundell, P. A., Le, N. P. L., Allen, J., Watanabe, Y., & Pleass, R. J.
- Affiliations
- Liverpool School of Tropical Medicine (GB)
- University of Oxford (GB)
- Corresponding author
- Pleass, Richard J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2017-08
- Volume
- 292
- Issue
- 31
- Pages
- 12994-13007
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5546038
- OpenAlex
- W2625138348
- Cited by
- 26
- References
- 47
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2023: 1 · 2022: 5 · 2021: 6 · 2020: 3 · 2019: 4 · 2018: 3
- FWCI
- 2.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (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 & 097830/Z/11/Z)
- 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
- Fc fusion protein, sialic acid, N-glycosylation, Fc receptors, complement system, multimerization, intravenous immunoglobulin replacement, sialylation, receptor binding
- MeSH terms
- Animals, Anti-Inflammatory Agents, Non-Steroidal, Asparagine, Cricetulus, Cystine, Glycosylation, Humans, Immunoglobulin G, Immunoglobulin Fc Fragments, Models, Molecular, Molecular Weight, Mutation, Protein Processing, Post-Translational, Receptors, Cell Surface, Recombinant Fusion Proteins, Recombinant Proteins, Drug Design, Protein Engineering, Molecular Structure, Mutagenesis, Site-Directed, CHO Cells, Amino Acid Substitution, Protein Interaction Domains and Motifs
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