Li Zihai
Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut School of Medicine, Farmington, CT 06030-1601, USA.
Methods. 2004 Jan;32(1):25-8. doi: 10.1016/s1046-2023(03)00183-x.
Known commonly as molecular chaperones for proteins, heat shock proteins (HSPs) have also been found to chaperone small molecular weight cellular peptides. HSP-peptide complexes can prime T cell immunity specific against the peptides bound to HSPs, but not against HSPs per se. This immunomodulatory functions of HSPs are based on two intrinsic properties. One, HSPs are excellent adjuvants due to their ability to activate dendritic cells (DCs). Two, HSPs can bind directly to their receptors on DCs to then channel HSP-associated peptides to associate with MHC molecules. When a specific antigenic peptide is defined, this peptide can also be complexed with either tissue derived or recombinant HSPs in vitro to generate HSP-peptide complexes as peptide-specific vaccines. This article focuses on the methods commonly used to reconstitute HSP-peptide complexes, and discusses assays to verify the efficiency of complexing for immunotherapy against cancers and infectious diseases.
热休克蛋白（HSPs）通常被称为蛋白质的分子伴侣，也被发现可辅助小分子细胞肽。HSP-肽复合物能够启动针对与HSPs结合的肽的特异性T细胞免疫，但不针对HSPs本身。HSPs的这种免疫调节功能基于两个内在特性。其一，HSPs因其激活树突状细胞（DCs）的能力而成为出色的佐剂。其二，HSPs可直接与其在DCs上的受体结合，进而引导与HSP相关的肽与MHC分子结合。当确定了特定的抗原肽后，该肽也可在体外与组织来源或重组的HSPs复合，以生成作为肽特异性疫苗的HSP-肽复合物。本文重点介绍了常用于重构HSP-肽复合物的方法，并讨论了验证针对癌症和传染病进行免疫治疗的复合效率的检测方法。
