I类主要组织相容性复合体（MHC）可将内源性肽呈递给细胞毒性T淋巴细胞。
Class I MHC can present an endogenous peptide to cytotoxic T lymphocytes.
作者信息
Whitton J L, Oldstone M B
机构信息
Research Institute of Scripps Clinic, La Jolla, California 92037.
出版信息
J Exp Med. 1989 Sep 1;170(3):1033-8. doi: 10.1084/jem.170.3.1033.
Abstract
Since class I MHC glycoproteins may function by "screening and selecting" degraded proteins, we wished to determine whether very short peptides made within a cell were detected and bound by MHC, and presented for T cell perusal. We show that a 22 amino acid viral sequence containing a Db-restricted nonameric CTL epitope is sufficient to direct CTL recognition/lysis of H2b target cells. The mechanism of epitope presentation is by the "natural" endogenous route, and appears to direct lysis as effectively as wild-type virus infection, in which the epitope is part of a 236 residue glycoprotein.
摘要
由于I类主要组织相容性复合体（MHC）糖蛋白可能通过“筛选和选择”降解的蛋白质发挥作用，我们希望确定细胞内产生的极短肽是否能被MHC检测和结合，并呈递给T细胞审视。我们发现，一个包含Db限制性九聚体CTL表位的22个氨基酸的病毒序列足以直接引导CTL识别/H2b靶细胞的裂解。表位呈递的机制是通过“天然”内源性途径，并且似乎与野生型病毒感染一样有效地直接导致裂解，在野生型病毒感染中，该表位是一个236个残基糖蛋白的一部分。
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