通过使蛋白质抗原与重组大热休克蛋白复合来增强抗原交叉呈递和T细胞启动。
Enhancing antigen cross-presentation and T-cell priming by complexing protein antigen to recombinant large heat-shock protein.
作者信息
Wang Xiang-Yang, Yi Huanfa, Yu Xiaofei, Zuo Damin, Subjeck John R
机构信息
Department of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular Medicine, Virginia Commonwealth University, Richmond, VA, USA.
出版信息
Methods Mol Biol. 2011;787:277-87. doi: 10.1007/978-1-61779-295-3_21.
Abstract
Large heat-shock proteins (HSPs), including hsp110 and grp170, are unique immunochaperones capable of carrying and introducing antigens into professional antigen-presenting cells for efficient cross-presentation. Therefore, reconstituted chaperone complexes of large HSPs and protein antigen may be exploited for augmentation of an antigen-specific immune response. The methods for the preparation of the recombinant protein antigen chaperone complex and characterization of its T-cell priming capability in both in vitro and in vivo settings are described.
摘要
大型热休克蛋白（HSPs），包括hsp110和grp170，是独特的免疫伴侣蛋白，能够携带抗原并将其导入专职抗原呈递细胞以实现高效的交叉呈递。因此，大型HSPs与蛋白质抗原重构的伴侣蛋白复合物可用于增强抗原特异性免疫反应。本文描述了重组蛋白抗原伴侣蛋白复合物的制备方法及其在体外和体内环境中T细胞启动能力的表征。
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