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.
CITATION STYLE
Wang, X. Y., 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 Methods in Molecular Biology (Vol. 787, pp. 277–287). Humana Press Inc. https://doi.org/10.1007/978-1-61779-295-3_21
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