Cutting edge

Cross-presentation of cell-associated antigens to MHC class I molecule is regulated by a major transcription factor for heat shock proteins

Hong Zheng, Zihai Li

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

The ability for the professional APC to cross-present Ag to MHC class I from parenchymal cells is essential for priming as well as tolerance of CD8 + T cells against intracellular Ags. Since cross-presentations of non-cell-associated free Ags are inefficient, the roles of molecular chaperones or heat shock proteins (HSPs) in chaperoning Ags to APCs have been postulated. We herein genetically addressed this hypothesis using mice that were defective of heat shock factor 1 (Hsf1), a major transcription factor for HSPs. Hsf1 -/- mice have a decreased expression of several HSPs including HSP90 and HSP70. Using multiple Ag systems, we demonstrated that cross-priming of Ag-specific CD8+ T cells was inefficient when Ag expression was restricted to Hsf1-/- non-APCs. Our study provides the first genetic evidence for the roles of Hsf1 in regulating cross-presentation of MHC class I-associated Ags.

Original languageEnglish (US)
Pages (from-to)5929-5933
Number of pages5
JournalJournal of Immunology
Volume173
Issue number10
DOIs
StatePublished - Nov 15 2004

Fingerprint

Cross-Priming
Heat-Shock Proteins
Shock
Transcription Factors
Hot Temperature
Antigens
T-Lymphocytes
HSP90 Heat-Shock Proteins
Molecular Chaperones
HSP70 Heat-Shock Proteins

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

@article{429c8bcecd6f46899cb722992d47bf6a,
title = "Cutting edge: Cross-presentation of cell-associated antigens to MHC class I molecule is regulated by a major transcription factor for heat shock proteins",
abstract = "The ability for the professional APC to cross-present Ag to MHC class I from parenchymal cells is essential for priming as well as tolerance of CD8 + T cells against intracellular Ags. Since cross-presentations of non-cell-associated free Ags are inefficient, the roles of molecular chaperones or heat shock proteins (HSPs) in chaperoning Ags to APCs have been postulated. We herein genetically addressed this hypothesis using mice that were defective of heat shock factor 1 (Hsf1), a major transcription factor for HSPs. Hsf1 -/- mice have a decreased expression of several HSPs including HSP90 and HSP70. Using multiple Ag systems, we demonstrated that cross-priming of Ag-specific CD8+ T cells was inefficient when Ag expression was restricted to Hsf1-/- non-APCs. Our study provides the first genetic evidence for the roles of Hsf1 in regulating cross-presentation of MHC class I-associated Ags.",
author = "Hong Zheng and Zihai Li",
year = "2004",
month = "11",
day = "15",
doi = "10.4049/jimmunol.173.10.5929",
language = "English (US)",
volume = "173",
pages = "5929--5933",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "10",

}

TY - JOUR

T1 - Cutting edge

T2 - Cross-presentation of cell-associated antigens to MHC class I molecule is regulated by a major transcription factor for heat shock proteins

AU - Zheng, Hong

AU - Li, Zihai

PY - 2004/11/15

Y1 - 2004/11/15

N2 - The ability for the professional APC to cross-present Ag to MHC class I from parenchymal cells is essential for priming as well as tolerance of CD8 + T cells against intracellular Ags. Since cross-presentations of non-cell-associated free Ags are inefficient, the roles of molecular chaperones or heat shock proteins (HSPs) in chaperoning Ags to APCs have been postulated. We herein genetically addressed this hypothesis using mice that were defective of heat shock factor 1 (Hsf1), a major transcription factor for HSPs. Hsf1 -/- mice have a decreased expression of several HSPs including HSP90 and HSP70. Using multiple Ag systems, we demonstrated that cross-priming of Ag-specific CD8+ T cells was inefficient when Ag expression was restricted to Hsf1-/- non-APCs. Our study provides the first genetic evidence for the roles of Hsf1 in regulating cross-presentation of MHC class I-associated Ags.

AB - The ability for the professional APC to cross-present Ag to MHC class I from parenchymal cells is essential for priming as well as tolerance of CD8 + T cells against intracellular Ags. Since cross-presentations of non-cell-associated free Ags are inefficient, the roles of molecular chaperones or heat shock proteins (HSPs) in chaperoning Ags to APCs have been postulated. We herein genetically addressed this hypothesis using mice that were defective of heat shock factor 1 (Hsf1), a major transcription factor for HSPs. Hsf1 -/- mice have a decreased expression of several HSPs including HSP90 and HSP70. Using multiple Ag systems, we demonstrated that cross-priming of Ag-specific CD8+ T cells was inefficient when Ag expression was restricted to Hsf1-/- non-APCs. Our study provides the first genetic evidence for the roles of Hsf1 in regulating cross-presentation of MHC class I-associated Ags.

UR - http://www.scopus.com/inward/record.url?scp=8444247044&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=8444247044&partnerID=8YFLogxK

U2 - 10.4049/jimmunol.173.10.5929

DO - 10.4049/jimmunol.173.10.5929

M3 - Article

VL - 173

SP - 5929

EP - 5933

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 10

ER -