| Literature DB >> 29177671 |
Chunqing Guo1,2,3, John R Subjeck4, Xiang-Yang Wang5,6,7.
Abstract
Large heat shock proteins (HSPs) or stress proteins, including Hsp110 and Grp170, are unique molecular chaperones with superior capability of shuttling tumor protein antigens into professional antigen-presenting cells, such as dendritic cells, for highly efficient cross-presentation and T cell priming. Reconstituted chaperone complexes of large HSP and tumor protein antigen have been demonstrated to generate a robust antigen-specific T lymphocyte response with therapeutic potency against multiple cancer types in preclinical models. Here, we describe the methods for preparing this recombinant chaperone complex vaccine and analyzing the vaccine-induced activation of antigen-specific T cells using in vitro and in vivo systems.Entities:
Keywords: Antigen cross-presentation; Chaperone vaccine; Grp170; Hsp110; Large heat shock protein; T cell activation
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Year: 2018 PMID: 29177671 PMCID: PMC5812279 DOI: 10.1007/978-1-4939-7477-1_25
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745