Enhancing antigen cross-presentation and T-cell priming by complexing protein antigen to recombinant large heat-shock protein.

Methods Mol Biol

Department of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular Medicine, Virginia Commonwealth University, Richmond, VA, USA.

Published: February 2012

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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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3271356PMC
http://dx.doi.org/10.1007/978-1-61779-295-3_21DOI Listing

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