Yang Y, Sempé P, Peterson P A
R.W. Johnson Pharmaceutical Research Institute, Scripps Research Institute, La Jolla, Calif 92037, USA.
Immunol Res. 1996;15(3):208-33. doi: 10.1007/BF02918250.
The presentation of antigenic peptides by class I major histocompatibility complex molecules plays a central role in the cellular immune response, since immune surveillance for detection of viral infections or malignant transformations is achieved by CD8+ T lymphocytes which inspect peptides, derived from intracellular proteins, bind to class I molecules on the surface of most cells. The transporter associated with antigen processing selectively translocates cytoplasmically derived peptides of appropriate sequence and length into the lumen of the endoplasmic reticulum where they associate with newly synthesized class I molecules. The translocated peptides are generated by multicatalytic and multisubunit proteasomes which degrade cytoplasmic proteins in a ATP-ubiquitin-dependent manner. This review discusses our current molecular understanding of class I antigen processing and presentation.
I类主要组织相容性复合体分子对抗原肽的呈递在细胞免疫反应中起核心作用,因为对病毒感染或恶性转化的免疫监视是通过CD8 + T淋巴细胞实现的,这些细胞检查源自细胞内蛋白质的肽,并与大多数细胞表面的I类分子结合。与抗原加工相关的转运体选择性地将具有适当序列和长度的细胞质衍生肽转运到内质网腔中,在那里它们与新合成的I类分子结合。转运的肽是由多催化和多亚基蛋白酶体产生的,这些蛋白酶体以ATP-泛素依赖性方式降解细胞质蛋白。本综述讨论了我们目前对I类抗原加工和呈递的分子理解。