Heat Shock Protein-Peptide Complexes as Anti-Viral Agents.

1997 ◽  
Author(s):  
CONNECTICUT UNIV HEALTH CENTER FARMINGTON
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Peptide Complexes

Anti-tumor effect of heat shock protein 70-Peptide complexes on A-549 cells

2007 ◽  
Vol 19 (3) ◽  
pp. 210-215 ◽  
Author(s):  
Hong-qi Wang ◽  
Chen-xia Hu ◽  
Ling Hu ◽  
Wei-xi Shen ◽  
Jian Zhao ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Peptide Complexes

BCG (Bacille Calmette–Guérin) HspCs (heat-shock protein–peptide complexes) induce T-helper 1 responses and protect against live challenge in a murine aerosol challenge model of pulmonary tuberculosis

2004 ◽  
Vol 32 (4) ◽  
pp. 626-628 ◽  
Author(s):  
C.A.L.S. Colaco ◽  
C.R. Bailey ◽  
J. Keeble ◽  
K.B. Walker
Keyword(s):  
Heat Shock ◽  
Pulmonary Tuberculosis ◽  
Immune Responses ◽  
Heat Shock Protein ◽  
T Helper ◽  
T Helper 1 ◽  
Bacille Calmette Guerin ◽  
Vaccine Candidates ◽  
Peptide Complexes ◽  
Further Development

The need for an effective TB (tuberculosis) vaccine remains acute, with tuberculosis still one of the major killers worldwide and 3 million new infections annually. We report here on the immune responses elicited by HspCs (heat-shock protein–peptide complexes) isolated from BCG (Bacille Calmette–Guérin) vaccine. These HspCs elicit both the appropriate cellular and protective immune responses required to merit their further development as TB vaccine candidates.

scholarly journals CD40, an extracellular receptor for binding and uptake of Hsp70–peptide complexes

2002 ◽  
Vol 158 (7) ◽  
pp. 1277-1285 ◽  
Author(s):  
Thalia Becker ◽  
F.-Ulrich Hartl ◽  
Felix Wieland
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Function ◽  
Surface Protein ◽  
Mhc I ◽  
Peptide Complex ◽  
Exogenous Hsp70 ◽  
A Cell ◽  
Peptide Complexes ◽  
Antigen Presenting

Tumor and viral antigens elicit a potent immune response by heat shock protein–dependent uptake of antigenic peptide with subsequent presentation by MHC I. Receptors on antigen-presenting cells that specifically bind and internalize a heat shock protein–peptide complex have not yet been identified. Here, we show that cells expressing CD40, a cell surface protein crucial for B cell function and autoimmunity, specifically bind and internalize human Hsp70 with bound peptide. Binding of Hsp70–peptide complex to the exoplasmic domain of CD40 is mediated by the NH2-terminal nucleotide–binding domain of Hsp70 in its ADP state. The Hsp70 cochaperone Hip, but not the bacterial Hsp70 homologue DnaK, competes formation of the Hsp70–CD40 complex. Binding of Hsp70-ADP to CD40 is strongly increased in the presence of Hsp70 peptide substrate, and induces signaling via p38. We suggest that CD40 is a cochaperone-like receptor mediating the uptake of exogenous Hsp70–peptide complexes by macrophages and dendritic cells.

scholarly journals Heat Shock Protein–Peptide Complexes, Reconstituted In Vitro, Elicit Peptide-specific Cytotoxic T Lymphocyte Response and Tumor Immunity

1997 ◽  
Vol 186 (8) ◽  
pp. 1315-1322 ◽  
Author(s):  
Nathalie E. Blachere ◽  
Zihai Li ◽  
Rajiv Y. Chandawarkar ◽  
Ryuichiro Suto ◽  
Navdeep S. Jaikaria ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
T Lymphocyte ◽  
Synthetic Peptides ◽  
Cytotoxic T Lymphocyte ◽  
T Cell Response ◽  
Lymphocyte Response ◽  
Peptide Complexes

Heat shock protein (HSP) preparations derived from cancer cells and virus-infected cells have been shown previously to elicit cancer-specific or virus-specific immunity. The immunogenicity of HSP preparations has been attributed to peptides associated with the HSPs. The studies reported here demonstrate that immunogenic HSP–peptide complexes can also be reconstituted in vitro. The studies show that (a) complexes of hsp70 or gp96 HSP molecules with a variety of synthetic peptides can be generated in vitro; (b) the binding of HSPs with peptides is specific in that a number of other proteins tested do not bind synthetic peptides under the conditions in which gp96 molecules do; (c) HSP–peptide complexes reconstituted in vitro are immunologically active, as tested by their ability to elicit antitumor immunity and specific CD8+ cytolytic T lymphocyte response; and (d) synthetic peptides reconstituted in vitro with gp96 are capable of being taken up and re-presented by macrophage in the same manner as gp96– peptides complexes generated in vivo. These observations demonstrate that HSPs are CD8+ T cell response–eliciting adjuvants.

Heat shock protein-peptide complexes for use in vaccines

1996 ◽  
Vol 60 (2) ◽  
pp. 153-158 ◽  
Author(s):  
Michael Heike ◽  
Bernhard Noll ◽  
Karl-Hermann Meyer zum Büschenfelde
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Peptide Complexes
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