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.
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Acknowledgments
This work was supported by National Institutes of Health Grants CA175033, CA154708, W81XWH-13-0455, and in part by National Cancer Institute (NCI) Cancer Center Support Grant to VCU Massey Cancer Center P30CA16059. X-Y.W. is the Mary Anderson Harrison Distinguished Professor in the VCU Massey Cancer Center.
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Guo, C., Subjeck, J.R., Wang, XY. (2018). Creation of Recombinant Chaperone Vaccine Using Large Heat Shock Protein for Antigen-Targeted Cancer Immunotherapy. In: Calderwood, S., Prince, T. (eds) Chaperones. Methods in Molecular Biology, vol 1709. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7477-1_25
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DOI: https://doi.org/10.1007/978-1-4939-7477-1_25
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