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.
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Acknowledgments
This work was supported by NIH research grants CA129111, CA154708, CA099326, and ACS RSG-08-187-01-LIB.
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Wang, XY., Yi, H., Yu, X., Zuo, D., Subjeck, J.R. (2011). Enhancing Antigen Cross-Presentation and T-Cell Priming by Complexing Protein Antigen to Recombinant Large Heat-Shock Protein. In: Calderwood, S., Prince, T. (eds) Molecular Chaperones. Methods in Molecular Biology, vol 787. Humana Press. https://doi.org/10.1007/978-1-61779-295-3_21
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DOI: https://doi.org/10.1007/978-1-61779-295-3_21
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