T cell activation by processed antigen is equally blocked by I-E and I-A-restricted immunodominant peptides.
T cell activation by processed antigen is equally blocked by I-E and I-A-restricted immunodominant peptides.
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I-E 和 I-A 限制性免疫显性肽同样会阻断加工抗原对 T 细胞的激活。
DOI：
10.1002/eji.1830171113
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发表时间：
1987
影响因子：
5.4
通讯作者：
Pierce,SK
中科院分区：
文献类型：
--
作者：
Lakey,EK;Casten,LA;Anderson,MS;Smolenski,LA;Smith,JA;Margoliash,E;Pierce,SK
T细胞对可溶性蛋白质的反应需要抗原提呈细胞(APC)将天然抗原处理成含有抗原决定簇的肽，该肽被运输到抗原提呈细胞表面并结合到抗原提呈细胞表面，在那里它随后被适当Ia分子背景下的特定T细胞识别。研究鸽子细胞色素c特异的IE k限制性T细胞杂交体的反应，它识别存在于10个氨基酸的蛋白质C末端片段中的决定簇，先前证明了与鸽子细胞色素c肽同源但没有刺激性的多肽，阻断了由APC加工和呈递的鸽子细胞色素c的T细胞反应。在这份报告中，一系列代表葡萄球菌核酸酶(Nase)全长的14个20个氨基酸的重叠多肽的能力被评估为它们阻止鸽子细胞色素c特异性T细胞杂交体对抗原冲击的提呈细胞的反应的能力。只有三个Nase多肽阻断了IE k限制性鸽子细胞色素c特异性T细胞反应。其中两个，Nase 61-80和Nase 91-110，在对Nase的IA d和IA b限制性反应中起T细胞抗原的作用。第三个封闭肽，Nase 101-120，还没有被证明是T细胞抗原。另外两个多肽，Nase 51-70和Nase 81-100，在IE k背景下被Nase特异性T细胞识别，但对IE k限制性细胞色素c特异性T细胞反应没有影响。这些多肽都不能阻断鸽子细胞色素c特异性T细胞对烟蛾细胞色素c的高亲和力和异质性反应。此外，来自三个不同物种的IE k限制性细胞色素c多肽也不能阻断IA k限制性T细胞对卵清蛋白的反应。因此，没有明显的初级氨基酸序列同源性，并且不能在同一Ia的背景下被识别的多肽，相互竞争APC上将处理的抗原呈递给T细胞所必需的位点。这些结果表明，除Ia外，APC表面还存在结构，这些结构是处理后有效的抗原提呈所必需的。这种细胞表面材料的一个合适的候选者是最近发现的肽结合蛋白PBP72/74(Lakey等人，Proc.娜塔莉。阿卡德。SCI。1987年美国。84：1659)。
The T cell response to a soluble protein requires the processing of the native antigen by an antigen-presenting cell (APC) to a peptide containing an antigenic determinant, which is transported to and bound on the antigen-presenting cell surface, where it is subsequently recognized by the specific T cell in the context of the appropriate Ia molecule. Investigating the response of a pigeon cytochrome c-specific, IE k-restricted T cell hybrid, which recognizes a determinant present within a 10-amino acid C-terminal fragment of the protein, it was previously demonstrated that peptides homologous to the peptide from pigeon cytochrome c, but which were not stimulatory, blocked the T cell response to pigeon cytochrome c as processed and presented by APC. In this report the ability of a series of fourteen, 20-amino acid overlapping peptides, representing the entire length of staphylococcal nuclease (Nase), were assessed for their ability to block the response of a pigeon cytochrome c-specific T cell hybrid to antigen-pulsed presenting cells. Only three Nase peptides blocked the IE k-restricted pigeon cytochrome c-specific T cell response. Two of these, Nase 61–80 and Nase 91–110, function as T cell antigens in the IA d and IA b-restricted response to Nase. The third blocking peptide, Nase 101–120, has not been shown to be a T cell antigen. Two other peptides, Nase 51–70 and Nase 81–100, which are recognized by Nase-specific T cells in the context of IE k, have no effect on the IE k-restricted cytochrome c-specific T cell response. None of these peptides block the higher affinity, heteroclitic response of pigeon cytochrome c-specific T cells to tobacco hornworm moth cytochrome c. Moreover, the response of an IA k-restricted T cell to ovalbumin was blocked by the IE k-restricted cytochrome c peptides from three different species. Thus, peptides with no obvious primary amino acid sequence homology, and which are not capable of being recognized in the context of the same Ia, compete with one another for the sites on the APC necessary for presentation of processed antigen to T cells. These results suggest that there are structures on the APC surface in addition to Ia, which are necessary for effective antigen presentation following processing. One suitable candidate for such a cell surface material is the recently identified peptide-binding protein, PBP72/74 (Lakey et al., Proc. Natl. Acad. Sci. USA 1987. 84: 1659).