Cited by 849Monoclonal and Polyclonal Antibodies ResearchGlycosylation and Glycoproteins ResearchT-cell and B-cell Immunology

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Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG Fc

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Anthony, Robert M., Nimmerjahn, Falk, Ashline, David J., Reinhold, Vernon N., Paulson, James C., Ravetch, Jeffrey V.·2008·Science

DOI 10.1126/science.1154315PMC PMC2409116

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Abstract

It is well established that high doses of monomeric immunoglobulin G (IgG) purified from pooled human plasma [intravenous immunoglobulin (IVIG)] confer anti-inflammatory activity in a variety of autoimmune settings. However, exactly how those effects are mediated is not clear because of the heterogeneity of IVIG. Recent studies have demonstrated that the anti-inflammatory activity of IgG is completely dependent on sialylation of the N-linked glycan of the IgG Fc fragment. Here we determine the precise glycan requirements for this anti-inflammatory activity, allowing us to engineer an appropriate IgG1 Fc fragment, and thus generate a fully recombinant, sialylated IgG1 Fc with greatly enhanced potency. This therapeutic molecule precisely defines the biologically active component of IVIG and helps guide development of an IVIG replacement with improved activity and availability.

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Authors: Anthony, R. M., Nimmerjahn, F., Ashline, D. J., Reinhold, V. N., Paulson, J. C., & Ravetch, J. V.
Affiliations: Scripps Research Institute (US)
Corresponding author: Ravetch, Jeffrey V.
ORCID: Anthony, Robert M.
Nimmerjahn, Falk
Paulson, James C.
Ravetch, Jeffrey V.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2008-04-18
Volume: 320
Issue: 5874
Pages: 373-376
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.1154315
PMC: PMC2409116
OpenAlex: W2051666192
Cited by: 849
References: 34
Citations by year: 2026: 19 · 2025: 32 · 2024: 29 · 2023: 37 · 2022: 39 · 2021: 39 · 2020: 50 · 2019: 39 · 2018: 45 · 2017: 46 · 2016: 66 · 2015: 58 · 2014: 58 · 2013: 58 · 2012: 68
FWCI: 42.36
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Science (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (5r01gm060938-10)
National Institute of General Medical Sciences (R01GM054045, R01-GM060938, GM60938)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
Keywords: intravenous immunoglobulin, anti-inflammatory activity, IgG Fc fragment, sialylation, N-glycans, glycan engineering, autoimmune disease
MeSH terms: Animals, Anti-Inflammatory Agents, Non-Steroidal, Arthritis, Experimental, Autoimmune Diseases, Carbohydrate Conformation, Galactose, Glycosylation, Humans, Immunoglobulin G, Immunoglobulin Fc Fragments, Mice, Inbred C57BL, Polysaccharides, Receptors, Fc, Recombinant Proteins, Purpura, Thrombocytopenic, Idiopathic, Mice, Inbred NOD, Immunoglobulins, Intravenous, N-Acetylneuraminic Acid, Mice

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Recapitulation of IVIG Anti-Inflammatory Activity with a Recombinant IgG Fc

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