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

  • Xiang-Yang Wang
  • Huanfa Yi
  • Xiaofei Yu
  • Damin Zuo
  • John R. Subjeck
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 787)

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 

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Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Xiang-Yang Wang
    • 1
  • Huanfa Yi
    • 1
  • Xiaofei Yu
    • 1
  • Damin Zuo
    • 1
  • John R. Subjeck
    • 2
  1. 1.Department of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular MedicineVirginia Commonwealth UniversityRichmondUSA
  2. 2.Department of Cellular Stress BiologyRoswell Park Cancer InstituteBuffaloUSA

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