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 |
| State | Published - 2000 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Immunology and Allergy
- Infectious Diseases
- Immunology
Cite this
A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins. / Cho, Bryan K.; Palliser, Deborah; Guillen, Eduardo; Wisniewski, Jan; Young, Richard A.; Chen, Jianzhu; Eisen, Herman N.
In: Immunity, Vol. 12, No. 3, 2000, p. 263-272.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A proposed mechanism for the induction of cytotoxic T lymphocyte production by heat shock fusion proteins
AU - Cho, Bryan K.
AU - Palliser, Deborah
AU - Guillen, Eduardo
AU - Wisniewski, Jan
AU - Young, Richard A.
AU - Chen, Jianzhu
AU - Eisen, Herman N.
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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UR - http://www.scopus.com/inward/citedby.url?scp=0033695064&partnerID=8YFLogxK
M3 - Article
C2 - 10755613
AN - SCOPUS:0033695064
VL - 12
SP - 263
EP - 272
JO - Immunity
JF - Immunity
SN - 1074-7613
IS - 3
ER -