热休克蛋白-多肽复合物在肿瘤和传染性疾病免疫中的作用

热休克蛋白家族中的许多成员如gp96\,HSP90\,HSP70等具有排斥和治疗肿瘤及传染性疾病的免疫原性，进一步研究发现热休克蛋白作为分子伴侣可结合细胞中的肽库，它本身没有抗原性，抗原性由结合的短肽所决定。热休克蛋白将结合的短肽呈递给I类MHC分子，进而激活特异性CTL和记忆性T细胞，引发机体细胞免疫反应。据最新发现gp96还可能有与MHC一样的功能，可直接将结合的多肽抗原呈递给T细胞。近年来对哺乳动物的二种主要热休克蛋白gp96和HSP70的免疫机制和作为治疗性疫苗的优越性进行了详细研究，这为乙型肝炎和乙肝继发性肝癌的免疫治疗提供了新思路。

Role of Heat Shock Protein-peptide Complexes on Tumor and Infectious Diseases Immunity

Many heat shock proteins, e.g. Gp96. HSP90, HSP70, etc have elicited rejection and immunotherapy immunogenicity of rumor and infectious diseases. Further study indicated that hsps can chaperone the endogenous repertoire of peptides, and the antigenicity of hsp-peptide complexes lies in the peptides, not HSPs. HSPs present peptides associated with them to MHC class I molecules for recognition by CTL and memory T cells, and elicit cellular immune responses. The lastest finding shows that gp96 may present antigenic peptides directly to T lymphoeytes functionally as MHC. In recent years the mechanism of immunogenicity and advantages as vaccine therapy of gp96 and HSP7O,the two main hsps in mammals have been studied in detail, which offers a new opportunity for immunotherapy of hepatitis B and hepatocellular carcinoma.