Extended O-GlcNAc on HLA Class-I-Bound Peptides
作者： Fabio Marino , Marshall Bern , Geert P. M. Mommen , Aneika C. Leney , Jacqueline A. M. van Gaans-van den Brink
DOI: 10.1021/JACS.5B06586
关键词:
摘要: We report unexpected mass spectrometric observations of glycosylated human leukocyte antigen (HLA) class I-bound peptides. Complemented by molecular modeling, in vitro enzymatic assays, and oxonium ion patterns, we propose that the observed O-linked glycans carrying up to five monosaccharides are extended O-GlcNAc's rather than GalNAc-initiated O-glycans. A cytosolic O-GlcNAc modification is normally terminal does not extend produce a polysaccharide, but on an HLA peptide presents special case because loaded I complex traffics through endoplasmic reticulum Golgi apparatus its way cell membrane hence exposed glycosyltransferases. also for first time natural presentation O- N-linked glycopeptides derived from proteins. peptides with centrally located oligosaccharides have been shown be immunogenic may thus important targets immune surveillance.
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