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Glycosylation and the immune system

Rudd, Pauline M., Elliott, Tim, Cresswell, Peter, Wilson, Ian A. and Dwek, Raymond A. (2001) Glycosylation and the immune system Science, 291, (5512), pp. 2370-2376. (doi:10.1126/science.291.5512.2370). (PMID:11269318).

Record type: Article

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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Published date: 2001

Identifiers

Local EPrints ID: 26583
URI: http://eprints.soton.ac.uk/id/eprint/26583
ISSN: 0036-8075
PURE UUID: 564350ef-cab4-4460-b949-3d5131ada85a
ORCID for Tim Elliott: ORCID iD orcid.org/0000-0003-1097-0222

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Date deposited: 20 Apr 2006
Last modified: 17 Jul 2017 16:07

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Contributors

Author: Pauline M. Rudd
Author: Tim Elliott ORCID iD
Author: Peter Cresswell
Author: Ian A. Wilson
Author: Raymond A. Dwek

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