Murshid Ayesha, Gong Jianlin, Calderwood Stuart K
Molecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
Boston University Medical School, Boston, MA, USA.
Methods Mol Biol. 2013;960:209-217. doi: 10.1007/978-1-62703-218-6_17.
The molecular chaperone heat-shock protein 70 (Hsp70) possesses immune stimulatory properties that have been employed in the preparation of anticancer vaccines. Hsp70 binds antigenic peptides in the cytoplasm of cancer cells. Hsp70 thus serves as a convenient, non-discriminating transporter of antigens and can protect the peptides during internalization by APC and cross presentation to T lymphocytes. We describe a method for purifying Hsp70-peptide complexes that can be used to prepare molecular chaperone-based vaccines, involving sequential gel filtration, ion exchange, and affinity chromatography.
分子伴侣热休克蛋白70（Hsp70）具有免疫刺激特性，已被用于制备抗癌疫苗。Hsp70在癌细胞的细胞质中结合抗原肽。因此，Hsp70可作为一种方便、无选择性的抗原转运体，并能在抗原呈递细胞（APC）内化过程中保护肽段，并将其交叉呈递给T淋巴细胞。我们描述了一种纯化Hsp70-肽复合物的方法，该方法可用于制备基于分子伴侣的疫苗，包括连续的凝胶过滤、离子交换和亲和色谱法。
