A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins

Bryan K. Cho; Deborah Palliser; Eduardo Guillen; Jan Wisniewski; Richard A. Young; Jianzhu Chen; Herman N. Eisen

doi:10.1016/S1074-7613(00)80179-X

A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins

Bryan K. Cho, Deborah Palliser, Eduardo Guillen, Jan Wisniewski, Richard A. Young, Jianzhu Chen, Herman N. Eisen

Research output: Contribution to journal › Article › peer-review

128 Scopus citations

Abstract

A 65 kDa mycobacterial heat shock protein (hsp65), fused to a polypeptide that contains an octapeptide (SIYRYYGL) agonist for a particular T cell receptor (2C TCR), stimulated C57BL/6 mice as well as CD4-deficient mice to produce CD8⁺ cytolytic T lymphocytes (CTL) to the fusion partner's octapeptide. This and other hsp65 fusion proteins but not native hsp65 itself stimulated dendritic cells in vitro and in vivo to upregulate the levels of MHC (class I and II) and costimulatory (B7.2) molecules. The results suggest a mechanism for the general finding that hsp fusion proteins, having fusion partners of widely differing lengths and sequences, elicit CD8 CTL to peptides from the fusion partners without requiring exogenous adjuvants or the participation of CD4⁺ T cells.

Original language	English (US)
Pages (from-to)	263-272
Number of pages	10
Journal	Immunity
Volume	12
Issue number	3
DOIs	https://doi.org/10.1016/S1074-7613(00)80179-X
State	Published - 2000
Externally published	Yes

ASJC Scopus subject areas

Immunology and Allergy
Immunology
Infectious Diseases

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title = "A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins",

abstract = "A 65 kDa mycobacterial heat shock protein (hsp65), fused to a polypeptide that contains an octapeptide (SIYRYYGL) agonist for a particular T cell receptor (2C TCR), stimulated C57BL/6 mice as well as CD4-deficient mice to produce CD8+ cytolytic T lymphocytes (CTL) to the fusion partner's octapeptide. This and other hsp65 fusion proteins but not native hsp65 itself stimulated dendritic cells in vitro and in vivo to upregulate the levels of MHC (class I and II) and costimulatory (B7.2) molecules. The results suggest a mechanism for the general finding that hsp fusion proteins, having fusion partners of widely differing lengths and sequences, elicit CD8 CTL to peptides from the fusion partners without requiring exogenous adjuvants or the participation of CD4+ T cells.",

author = "Cho, {Bryan K.} and Deborah Palliser and Eduardo Guillen and Jan Wisniewski and Young, {Richard A.} and Jianzhu Chen and Eisen, {Herman N.}",

note = "Funding Information: We are grateful to Carol McKinley for skillful technical help; Nir Hacohen for advice about dendritic cells; Glenn Paradis for help with flow cytometry; Richard Cook of the MIT biopolymer laboratory for peptide synthesis, amino acid analyses, and mass spectrometry; Evelyn Wiebe for endotoxin assays; and Jun Liu and Satoshi Sugawa for helpful discussions. We are grateful to Vical for the VR1055 plasmid. B. K. C. was supported by a National Institutes of Health training grant (5T32-AI-07463) and D. P. by a Stressgen postdoctoral fellowship. This work was supported in part by a National Institutes of Health Cancer Center core grant (CA-14051) and National Institutes of Health research grants (CA-60686, AI-44477, and AI-44478).",

year = "2000",

doi = "10.1016/S1074-7613(00)80179-X",

language = "English (US)",

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AU - Cho, Bryan K.

AU - Palliser, Deborah

AU - Guillen, Eduardo

AU - Wisniewski, Jan

AU - Young, Richard A.

AU - Chen, Jianzhu

AU - Eisen, Herman N.

N1 - Funding Information: We are grateful to Carol McKinley for skillful technical help; Nir Hacohen for advice about dendritic cells; Glenn Paradis for help with flow cytometry; Richard Cook of the MIT biopolymer laboratory for peptide synthesis, amino acid analyses, and mass spectrometry; Evelyn Wiebe for endotoxin assays; and Jun Liu and Satoshi Sugawa for helpful discussions. We are grateful to Vical for the VR1055 plasmid. B. K. C. was supported by a National Institutes of Health training grant (5T32-AI-07463) and D. P. by a Stressgen postdoctoral fellowship. This work was supported in part by a National Institutes of Health Cancer Center core grant (CA-14051) and National Institutes of Health research grants (CA-60686, AI-44477, and AI-44478).

PY - 2000

Y1 - 2000

N2 - A 65 kDa mycobacterial heat shock protein (hsp65), fused to a polypeptide that contains an octapeptide (SIYRYYGL) agonist for a particular T cell receptor (2C TCR), stimulated C57BL/6 mice as well as CD4-deficient mice to produce CD8+ cytolytic T lymphocytes (CTL) to the fusion partner's octapeptide. This and other hsp65 fusion proteins but not native hsp65 itself stimulated dendritic cells in vitro and in vivo to upregulate the levels of MHC (class I and II) and costimulatory (B7.2) molecules. The results suggest a mechanism for the general finding that hsp fusion proteins, having fusion partners of widely differing lengths and sequences, elicit CD8 CTL to peptides from the fusion partners without requiring exogenous adjuvants or the participation of CD4+ T cells.

AB - A 65 kDa mycobacterial heat shock protein (hsp65), fused to a polypeptide that contains an octapeptide (SIYRYYGL) agonist for a particular T cell receptor (2C TCR), stimulated C57BL/6 mice as well as CD4-deficient mice to produce CD8+ cytolytic T lymphocytes (CTL) to the fusion partner's octapeptide. This and other hsp65 fusion proteins but not native hsp65 itself stimulated dendritic cells in vitro and in vivo to upregulate the levels of MHC (class I and II) and costimulatory (B7.2) molecules. The results suggest a mechanism for the general finding that hsp fusion proteins, having fusion partners of widely differing lengths and sequences, elicit CD8 CTL to peptides from the fusion partners without requiring exogenous adjuvants or the participation of CD4+ T cells.

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A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins

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