一种普遍存在的蛋白质是天然存在的肽的来源，这些肽可被一个CD8 + T细胞克隆识别。
A ubiquitous protein is the source of naturally occurring peptides that are recognized by a CD8+ T-cell clone.
作者信息
Udaka K, Tsomides T J, Walden P, Fukusen N, Eisen H N
机构信息
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
出版信息
Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11272-6. doi: 10.1073/pnas.90.23.11272.
Abstract
We previously isolated from mouse spleen an octapeptide (LSPFPFDL) that in association with the class I major histocompatibility complex protein Ld is recognized by the antigen-specific receptor of an alloreactive CD8+ T-cell clone (2C). Guided by an assay dependent upon the same 2C T-cell receptor, we have now isolated from the same source another naturally occurring peptide. The second peptide (VAITRIEQLSPFPFDL) includes the entire octapeptide sequence and preliminary evidence suggests that it may be a natural precursor of the octapeptide. On finding extensive sequence homology between the 16-mer and part of human 2-oxoglutarate dehydrogenase, we determined the cDNA sequence of mouse 2-oxoglutarate dehydrogenase and found that the deduced amino acid sequence matches precisely the two naturally occurring peptides, indicating their origin by cellular processing of this ubiquitous self protein.
摘要
我们之前从小鼠脾脏中分离出一种八肽（LSPFPFDL），该八肽与I类主要组织相容性复合体蛋白Ld结合时，能被同种异体反应性CD8⁺ T细胞克隆（2C）的抗原特异性受体识别。在一种依赖于相同2C T细胞受体的检测方法的指导下，我们现在又从同一来源分离出另一种天然存在的肽。第二种肽（VAITRIEQLSPFPFDL）包含了整个八肽序列，初步证据表明它可能是该八肽的天然前体。在发现这种16聚体与人类2-氧代戊二酸脱氢酶的一部分存在广泛的序列同源性后，我们测定了小鼠2-氧代戊二酸脱氢酶的cDNA序列，发现推导的氨基酸序列与这两种天然存在的肽精确匹配，表明它们是通过对这种普遍存在的自身蛋白进行细胞加工而产生的。
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