A MECHANISM FOR THE SPECIFIC IMMUNOGENICITY OF HEAT-SHOCK PROTEIN-CHAPERONED PEPTIDES
A MECHANISM FOR THE SPECIFIC IMMUNOGENICITY OF HEAT-SHOCK PROTEIN-CHAPERONED PEPTIDES
复制标题
DOI：
10.1126/science.7545313
复制
发表时间：
1995-09-15
期刊：
影响因子：
56.9
通讯作者：
SRIVASTAVA, PK
中科院分区：
文献类型：
--
作者：
SUTO, R;SRIVASTAVA, PK
内源合成的抗原决定簇通常呈递在主要组织相容性复合物(MHC) I类分子上，而外源决定簇则由MHC II类分子呈递。在此，研究表明，由热休克蛋白陪伴的外源抗原可以引导至内源途径，由 MHC I 类分子呈递，并被 CD8(+) T 淋巴细胞识别。该途径仅在所测试的细胞类型中的一部分巨噬细胞中起作用。这些观察结果为同源热休克蛋白制剂的肿瘤特异性和病毒特异性免疫原性提供了基础，并为交叉引发的经典现象提供了机制。
Endogenously synthesized antigenic determinants are generally presented on major histocompatibility complex (MHC) class I molecules, whereas exogenous determinants are presented by MHC class II molecules. Here, it is shown that exogenous antigens chaperoned by a heat shock protein can be channeled into the endogenous pathway, presented by MHC class I molecules, and recognized by CD8(+) T lymphocytes. This pathway is functional only in a subset of macrophages among the cell types tested. These observations provide a basis for the tumor-specific and virus-specific immunogenicity of cognate heat shock protein preparations and offer a mechanism for the classical phenomenon of cross-priming.