Wang Xiang-Yang, Manjili Masoud H, Park Juneui, Chen Xing, Repasky Elizabeth, Subjeck John R
Department of Molecular and Cellular Biophysics, Roswell Park Cancer Institute, Buffalo, NY 14263, USA.
Methods. 2004 Jan;32(1):13-20. doi: 10.1016/s1046-2023(03)00181-6.
High molecular weight heat shock proteins (HSPs), hsp110 and grp170, derived from cancer cells have been previously shown to elicit tumor-specific immunity. This phenomenon is attributed to the antigenic peptides associated with the HSPs. Based on the unique chaperoning properties of these HSPs, a new vaccination strategy has been recently developed to elicit antigen-specific antitumor immunity. This approach utilizes tumor-associated antigens naturally complexed to these highly efficient molecular chaperones under heat shock conditions. This chapter focuses on the methodologies of these two vaccine strategies: I. purification of hsp110 and grp170 from tumor tissue or cell lines; II. generation and characterization of in vitro HSP-antigen complexes by heat shock using recombinant HSPs derived from a baculovirus protein expression system.
高分子量热休克蛋白（HSPs），即hsp110和grp170，源自癌细胞，此前已被证明可引发肿瘤特异性免疫。这种现象归因于与热休克蛋白相关的抗原肽。基于这些热休克蛋白独特的伴侣功能，最近开发了一种新的疫苗接种策略来引发抗原特异性抗肿瘤免疫。该方法利用在热休克条件下与这些高效分子伴侣自然复合的肿瘤相关抗原。本章重点介绍这两种疫苗策略的方法：一、从肿瘤组织或细胞系中纯化hsp110和grp170；二、使用源自杆状病毒蛋白表达系统的重组热休克蛋白通过热休克在体外生成和表征热休克蛋白-抗原复合物。
