Yewdell J W, Esquivel F, Arnold D, Spies T, Eisenlohr L C, Bennink J R
Laboratory of Viral Diseases, National Institute of Allergy and Infections Diseases, National Institutes of Health, Bethesda, Maryland 20892.
J Exp Med. 1993 Jun 1;177(6):1785-90. doi: 10.1084/jem.177.6.1785.
The major histocompatibility complex-encoded transporter associated with antigen processing (TAP) is required for the efficient presentation of cytosolic antigens to class I-restricted T cells. TAP is thought to be formed by the interaction of two gene products, termed TAP1 and TAP2. We find that TAPs consisting either of human subunits, or mouse TAP1 and human TAP2, facilitate the presentation of numerous defined viral peptides to mouse class I-restricted T cells. As human and mouse TAP2 and TAP1 differ in 23 and 28% of their residues, respectively, this indicates that TAP1 and TAP2 can form a functional complex with partners considerably different from those they coevolved with. Moreover, these findings indicate that widely disparate TAPs facilitate delivery of the same peptides to class I molecules. These findings suggest that TAP polymorphism does not greatly influence the types of peptides presented to the immune system.
与抗原加工相关的主要组织相容性复合体编码转运体(TAP)是将胞质抗原有效呈递给I类限制性T细胞所必需的。TAP被认为是由两种基因产物TAP1和TAP2相互作用形成的。我们发现,由人类亚基组成的TAP,或小鼠TAP1和人类TAP2组成的TAP,都能促进将多种确定的病毒肽呈递给小鼠I类限制性T细胞。由于人类和小鼠的TAP2和TAP1分别有23%和28%的氨基酸残基不同,这表明TAP1和TAP2可以与与其共同进化的伙伴有很大差异的伙伴形成功能复合体。此外,这些发现表明,差异很大的TAP能促进将相同的肽递送至I类分子。这些发现表明,TAP多态性对呈递给免疫系统的肽的类型影响不大。