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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Animals
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Antigen Presentation / immunology*
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Antigen-Presenting Cells / immunology
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Baculoviridae / genetics
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Baculoviridae / metabolism
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Cancer Vaccines / immunology
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Cross-Priming / immunology
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Glycoproteins / immunology*
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Glycoproteins / metabolism
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HSP110 Heat-Shock Proteins / immunology*
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HSP110 Heat-Shock Proteins / metabolism
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HSP70 Heat-Shock Proteins / immunology*
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HSP70 Heat-Shock Proteins / metabolism
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Humans
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Lymphocyte Activation / immunology*
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Mice
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Mice, Transgenic
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Molecular Chaperones / immunology
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Protein Folding
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Recombinant Proteins / immunology
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T-Lymphocytes / immunology*
Substances
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Cancer Vaccines
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Glycoproteins
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HSP110 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins
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Molecular Chaperones
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Recombinant Proteins
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glucose-regulated protein 170