期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2020
卷号：117
期号：32
页码：19399-19407
DOI：10.1073/pnas.2004372117
出版社：The National Academy of Sciences of the United States of America
摘要：The source proteins from which CD8 T cell-activating peptides are derived remain enigmatic. Glycoproteins are particularly challenging in this regard owing to several potential trafficking routes within the cell. By engineering a glycoprotein-derived epitope to contain an N-linked glycosylation site, we determined that optimal CD8 T cell expansion and function were induced by the peptides that are rapidly produced from the exceedingly minor fraction of protein mislocalized to the cytosol. In contrast, peptides derived from the much larger fraction that undergoes translocation and quality control are produced with delayed kinetics and induce suboptimal CD8 T cell responses. This dual system of peptide generation enhances CD8 T cell participation in diversifying both antigenicity and the kinetics of peptide display.
关键词：antigen presentation ; MHC class I ; CD8 T cell ; DRiP ; signal sequence
