MHC I级
内质网
与抗原处理相关的转运体
生物
主要组织相容性复合体
抗原处理
CD8型
氨肽酶
抗原呈递
MHC限制
细胞毒性T细胞
肽
表位
抗原
人口
细胞生物学
分子生物学
生物化学
氨基酸
免疫学
亮氨酸
体外
人口学
社会学
作者
Nicolas Blanchard,Takayuki Kanaseki,Hernando Criollo Escobar,Frédéric Delebecque,Niranjana Nagarajan,Eduardo Reyes‐Vargas,David K. Crockett,David H. Raulet,Julio Delgado,Nilabh Shastri
出处
期刊:Journal of Immunology
[The American Association of Immunologists]
日期:2010-03-15
卷期号:184 (6): 3033-3042
被引量:81
标识
DOI:10.4049/jimmunol.0903712
摘要
The MHC class I (MHC-I) molecules ferry a cargo of peptides to the cell surface as potential ligands for CD8(+) cytotoxic T cells. For nearly 20 years, the cargo has been described as a collection of short 8-9 mer peptides, whose length and sequences were believed to be primarily determined by the peptide-binding groove of MHC-I molecules. Yet the mechanisms for producing peptides of such optimal length and composition have remained unclear. In this study, using mass spectrometry, we determined the amino acid sequences of a large number of naturally processed peptides in mice lacking the endoplasmic reticulum aminopeptidase associated with Ag processing (ERAAP). We find that ERAAP-deficiency changed the oeuvre and caused a marked increase in the length of peptides normally presented by MHC-I. Furthermore, we observed similar changes in the length of viral peptides recognized by CD8(+) T cells in mouse CMV-infected ERAAP-deficient mice. In these mice, a distinct CD8(+) T cell population was elicited with specificity for an N-terminally extended epitope. Thus, the characteristic length, as well as the composition of MHC-I peptide cargo, is determined not only by the MHC-I peptide-binding groove but also by ERAAP proteolysis in the endoplasmic reticulum.
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