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Molecular Chaperones

Volume 787 of the series Methods in Molecular Biology pp 277-287

Date:

Enhancing Antigen Cross-Presentation and T-Cell Priming by Complexing Protein Antigen to Recombinant Large Heat-Shock Protein

  • Xiang-Yang WangAffiliated withDepartment of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular Medicine, Virginia Commonwealth University Email author 
  • , Huanfa YiAffiliated withDepartment of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular Medicine, Virginia Commonwealth University
  • , Xiaofei YuAffiliated withDepartment of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular Medicine, Virginia Commonwealth University
  • , Damin ZuoAffiliated withDepartment of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular Medicine, Virginia Commonwealth University
  • , John R. SubjeckAffiliated withDepartment of Cellular Stress Biology, Roswell Park Cancer Institute

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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.

Key words

Large heat-shock protein hsp110 grp170 Chaperone vaccine Antigen presentation T-cell priming