Glycosylation and the Immune System
Abstract
Almost all of the key molecules involved in the innate and adaptive immune response are glycoproteins. In the cellular immune system, specific glycoforms are involved in the folding, quality control, and assembly of peptide-loaded major histocompatibility complex (MHC) antigens and the T cell receptor complex. Although some glycopeptide antigens are presented by the MHC, the generation of peptide antigens from glycoproteins may require enzymatic removal of sugars before the protein can be cleaved. Oligosaccharides attached to glycoproteins in the junction between T cells and antigen-presenting cells help to orient binding faces, provide protease protection, and restrict nonspecific lateral protein-protein interactions. In the humoral immune system, all of the immunoglobulins and most of the complement components are glycosylated. Although a major function for sugars is to contribute to the stability of the proteins to which they are attached, specific glycoforms are involved in recognition events. For example, in rheumatoid arthritis, an autoimmune disease, agalactosylated glycoforms of aggregated immunoglobulin G may induce association with the mannose-binding lectin and contribute to the pathology.
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- Authors
- Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A., & Dwek, R. A.
- Affiliations
- University of Oxford (GB)
- Southampton General Hospital (GB)
- Howard Hughes Medical Institute (US)
- Scripps Research Institute (US)
- Corresponding author
- Rudd, Pauline M.
- Dwek, Raymond A.
- Venue
- Science
- Published
- 2001-03-23
- Volume
- 291
- Issue
- 5512
- Pages
- 2370-2376
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1992886596
- Cited by
- 1,588
- References
- 3
- Citations by year
- 2026: 34 · 2025: 53 · 2024: 42 · 2023: 53 · 2022: 53 · 2021: 67 · 2020: 59 · 2019: 61 · 2018: 68 · 2017: 64 · 2016: 66 · 2015: 81 · 2014: 78 · 2013: 85 · 2012: 79
- FWCI
- 4.42
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (submittedVersion)
- Funders
- National Cancer Institute (R01CA058896, CA 58896)
- National Institute of Allergy and Infectious Diseases (AI42266)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Keywords
- glycosylation, immune system, glycoproteins, T cell receptor complex, immunoglobulin glycosylation, complement proteins, mannose-binding lectin, rheumatoid arthritis, oligosaccharides, antigen-presenting cells, innate immunity, adaptive immunity
- MeSH terms
- Animals, Antigen-Antibody Reactions, Antigen-Presenting Cells, Epitopes, Carrier Proteins, Complement System Proteins, Endoplasmic Reticulum, Glycoproteins, Glycosylation, Histocompatibility Antigens, Humans, Immune System, Immunoglobulins, Polysaccharides, T-Lymphocytes, Viral Envelope Proteins, Protein Folding, Antigen Presentation, Antigens, CD1, Collectins
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