内质网中主要组织相容性复合体I类限制抗原的加工
Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum.
作者信息
Elliott T, Willis A, Cerundolo V, Townsend A
机构信息
Institute for Molecular Medicine, John Radcliffe Hospital, Oxford, United Kingdom.
出版信息
J Exp Med. 1995 Apr 1;181(4):1481-91. doi: 10.1084/jem.181.4.1481.
Abstract
We have introduced long precursor peptides directly into the endoplasmic reticulum (ER) of a mutant cell line (T2-Db) that lacks the ability to transport peptides from the cytosol to the ER in a transporter associated with antigen processing (TAP) dependent way. This was done by expressing various influenza A-derived peptides containing the naturally processed epitope ASNENMDAM (366-374) preceded by the influenza hemagglutinin ER translocation sequence. Peptides derived from these minigenes that became associated with Db were isolated and identified by combined reversed phase liquid chromatography and detection by cytotoxic T lymphocytes. Our results establish that NH2-terminal extensions of at least 40 residues can be trimmed from peptides entering the ER, but that proteolysis of larger proteins may be limited.
摘要
我们已将长前体肽直接导入一种突变细胞系（T2-Db）的内质网（ER）中，该细胞系缺乏以与抗原加工相关的转运体（TAP）依赖方式将肽从胞质溶胶转运至内质网的能力。这是通过表达各种源自甲型流感病毒的肽来实现的，这些肽含有天然加工的表位ASNENMDAM（366 - 374），且前面带有流感血凝素内质网转运序列。通过反相液相色谱联用细胞毒性T淋巴细胞检测，分离并鉴定了源自这些小基因且与Db相关的肽。我们的结果表明，进入内质网的肽的至少40个残基的NH2末端延伸可以被修剪，但更大蛋白质的蛋白水解可能受到限制。
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