HLA-A2.1-ASSOCIATED PEPTIDES FROM A MUTANT-CELL LINE - A 2ND PATHWAY OF ANTIGEN PRESENTATION
HLA-A2.1-ASSOCIATED PEPTIDES FROM A MUTANT-CELL LINE - A 2ND PATHWAY OF ANTIGEN PRESENTATION
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DOI：
10.1126/science.1546329
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发表时间：
1992-03-06
期刊：
影响因子：
56.9
通讯作者：
ENGELHARD, VH
中科院分区：
文献类型：
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作者：
HENDERSON, RA;MICHEL, H;ENGELHARD, VH
从抗原处理突变体CEMx721.174.T2表达的人类白细胞抗原-A2.1-I类主要组织相容性复合体(MHC)分子中提取多肽，用电喷雾电离串联质谱仪进行鉴定。只发现了7个优势多肽，而正常细胞上有200多个与HLA-A2.1相关的多肽。这些多肽来源于正常细胞蛋白的信号肽结构域，通常大于9个残基，在正常细胞中也与人类白细胞抗原-A2.1相关。这些结果表明，内质网中信号肽域的蛋白分解是处理和呈递与I类分子相关的多肽的第二种机制。
Peptides extracted from HLA-A2.1 class I major histocompatibility complex (MHC) molecules expressed on the antigen processing mutant CEMx721.174.T2 were characterized by electrospray ionization-tandem mass spectrometry. Only seven dominant peptides were found, in contrast to over 200 associated with HLA-A2.1 on normal cells. These peptides were derived from the signal peptide domains of normal cellular proteins, were usually larger than nine residues, and were also associated with HLA-A2.1 in normal cells. These results suggest that proteolysis of signal peptide domains in the endoplasmic reticulum is a second mechanism for processing and presentation of peptides for association with class I molecules.