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

Xiang-Yang Wang1, Huanfa Yi, Xiaofei Yu

  • 1Department of Human and Molecular Genetics, Massey Cancer Center, Institute of Molecular Medicine, Virginia Commonwealth University, Richmond, VA, USA. xywang@vcu.edu

Methods in Molecular Biology (Clifton, N.J.)
|September 8, 2011
PubMed

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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