Sercarz Eli E, Maverakis Emanual
Torrey Pines Institute for Molecular Studies, San Diego, California 92121, USA.
Nat Rev Immunol. 2003 Aug;3(8):621-9. doi: 10.1038/nri1149.
Ever since the emergence of models for the processing and presentation of antigenic determinants by MHC class II molecules, the main view has been that proteins are unfolded, enzymatically cleaved into peptide lengths of about 12-25 amino acids and then loaded onto MHC class II molecules. There is, however, an alternative model stating that partially intact unfolding antigens are first bound by MHC class II molecules and then trimmed to fragments of a smaller size while remaining bound to the MHC class II molecule. In this analysis, we make the case that a considerable portion of the elutable peptide cargo belongs to this latter class.
自从出现了关于MHC II类分子对抗原决定簇进行加工和呈递的模型以来，主要观点一直认为蛋白质会发生解折叠，经酶切形成长度约为12 - 25个氨基酸的肽段，然后加载到MHC II类分子上。然而，存在另一种模型，该模型指出部分完整的未折叠抗原首先与MHC II类分子结合，然后在保持与MHC II类分子结合的同时被修剪成更小的片段。在本分析中，我们认为可洗脱肽负载的相当一部分属于后一类。
