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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.

Original publication

DOI

10.1126/science.291.5512.2370

Type

Journal article

Journal

Science (New York, N.Y.)

Publication Date

03/2001

Volume

291

Pages

2370 - 2376

Addresses

The Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. pmr@glycob.ox.ac.uk

Keywords

Antigen-Presenting Cells, T-Lymphocytes, Endoplasmic Reticulum, Immune System, Animals, Humans, Glycoproteins, Polysaccharides, Immunoglobulins, Carrier Proteins, Collectins, Viral Envelope Proteins, Antigens, CD1, Histocompatibility Antigens, Epitopes, Antigen-Antibody Reactions, Antigen Presentation, Protein Folding, Glycosylation, Complement System Proteins