The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
Abstract
A monoclonal human IgG1, Campath-1H, was digested with glycosidases to assess the effect of carbohydrate on the functional activities of an IgG1. Removal of the complete carbohydrate moiety abolished complement lysis activity and antibody-dependent cell-mediated cytotoxicity, but left antigen binding activity and protein A binding activity intact. Removal of terminal sialic acid residues through glycopeptidase F digestion was not found to affect any of the tested IgG activities. Removal of the majority of the galactose residues from desialylated Campath-1H was found to reduce but not abolish complement lysis activity. Other activities were not affected by degalactosylation. This indicates a rare separation of complement lysis activity and antibody-dependent cell-mediated cytotoxicity of IgG in the way they behave under controlled conditions. This paper underlines the overall importance of carbohydrate in IgG function and stresses the relative contributions of some of the carbohydrate residues.
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Enriching the abundance of mAb N-glycoforms with β1,4-linked galactose can enhance complement-dependent cytotoxicity (CDC).
“Enriching the abundance of mAb N-glycoforms with β1,4-linked galactose (Gal) can also be desirable as it has been shown to enhance complement-dependent cytotoxicity (CDC), another mechanism for the selective depletion of tumour cells by Fc activation of the complement pathway [16–21].”
From Glycoengineering Chinese hamster ovary cells: a short history (2021) · cites this paper as [21]
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References 22 · Cited by 283
- Authors
- Boyd, P. N., Lines, A. C., & Patel, A. K.
- Affiliations
- Wellcome Trust (GB)
- ORCID
- Patel, A.K.
- Venue
- Molecular Immunology
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 32
- Issue
- 17-18
- Pages
- 1311-1318
- ISSN
- 0161-5890 (ISSN-L)
- OpenAlex
- W2065419141
- Cited by
- 283
- References
- 22
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 11 · 2023: 6 · 2022: 6 · 2021: 16 · 2020: 15 · 2019: 11 · 2018: 20 · 2017: 12 · 2016: 14 · 2015: 10 · 2014: 18 · 2013: 19 · 2012: 16
- FWCI
- 1.11
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular Immunology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Immunology and Microbiology › Immunology › Complement system in diseases
- Keywords
- Campath-1H, anti-CD3 monoclonal antibody, IgG1, sialic acid, galactose, desialylation, complement-mediated lysis, antibody-dependent cellular cytotoxicity, glycosidase digestion, antigen binding, protein A binding
- MeSH terms
- Alemtuzumab, Amidohydrolases, Animals, Antibodies, Monoclonal, Antibodies, Neoplasm, Antibody-Dependent Cell Cytotoxicity, Carbohydrate Sequence, Complement System Proteins, Cytotoxicity Tests, Immunologic, Galactose, Cricetinae, Humans, Immunoglobulin G, Molecular Sequence Data, Multiple Myeloma, Neuraminidase, Sialic Acids, Structure-Activity Relationship, Tumor Cells, Cultured, CHO Cells, N-Acetylneuraminic Acid, Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, Antibodies, Monoclonal, Humanized
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