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Presentation of cytosolic glycosylated peptides by human class I major histocompatibility complex molecules in vivo

AuthorsHaurum, John S.; Høier, Ingelise Bjerring; Arsequell, Gemma ; Neisig, Anne; Valencia Parera, Gregorio; Zeuthen, Jesper; Neefjes, Jacques; Elliott, Tim
Class I histocompatibility antigens
Posttranslational protein processing
Antigen presentation
Issue Date5-Jul-1999
PublisherRockefeller University Press
CitationJournal of Experimental Medicine 190(1):145-150 (1999)
AbstractAntigens presented by class I major histocompatibility complex (MHC) molecules for recognition by cytotoxic T lymphocytes consist of 8-10-amino-acid-long cytosolic peptides. It is not known whether posttranslationally modified peptides are also presented by class I MHC molecules in vivo. Many different posttranslational modifications occur on cytoplasmic proteins, including a cytosolic O-beta-linked glycosylation of serine and threonine residues with N-acetylglucosamine (GlcNAc). Using synthetic glycopeptides carrying the monosaccharide O-beta-GlcNAc substitution on serine residues, we have shown that glycopeptides bind efficiently to class I MHC molecules and elicit a glycopeptide-specific cytotoxic T lymphocyte response in mice. In this study, we provide evidence that peptides presented by human class I MHC molecules in vivo encompass a small, significant amount of glycopeptides, constituting up to 0.1% of total peptide. Furthermore, we find that carbohydrate structures present on glycopeptides isolated from class I MHC molecules are dominated by the cytosolic O-beta-GlcNAc substitution, and synthetic peptides carrying this substitution are efficiently transported by TAP (transporter associated with antigen presentation) into the endoplasmic reticulum. Thus, in addition to unmodified peptides, posttranslationally modified cytosolic peptides carrying O-beta-linked GlcNAc can be presented by class I MHC molecules to the immune system.
Description6 pages, 4 figures.-- PMID: 10429679 [PubMed].-- PMCID: PMC2195561.
Publisher version (URL)http://dx.doi.org/10.1084/jem.190.1.145
Appears in Collections:(IQAC) Artículos
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