Document Detail


Phylogenetic conservation of the molecular and immunological properties of the chaperones gp96 and hsp70.
MedLine Citation:
PMID:  11265634     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The heat shock proteins (HSP) gp96 and hsp70 have been shown to have a critical role in eliciting adaptive immune responses to cancers and viruses. This role derives from (i) their ability to chaperone antigenic peptides generated in the cells from which the HSP are isolated, and (ii) their capacity to interact with antigen presenting cells (APC) which re-present the HSP-chaperoned peptides in context of MHC I molecules. We have asked whether the immunological properties of HSP extend beyond the mammals to other phyla. We report here the serological, biochemical, genetic, and immunological characterization of the Xenopus gp96. Like mammalian gp96, Xenopus gp96 forms non-covalent complexes with peptides. Immunization with gp96 and hsp70 purified from Xenopus tumors, elicits potent and specific anti-tumor immunity, which is dependent on their ability to chaperone peptides in vivo. An immunogenic peptide chaperoned by the Xenopus gp96 can be processed and presented by mouse APC, to antigen-specific CD8+ T cells of mice. The remarkable conservation of these essential immunological properties of gp96 and hsp70 between amphibians and mammals suggests the importance of HSP in the evolution of the vertebrate immune system.
Authors:
J Robert; A Ménoret; S Basu; N Cohen; P R Srivastava
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  European journal of immunology     Volume:  31     ISSN:  0014-2980     ISO Abbreviation:  Eur. J. Immunol.     Publication Date:  2001 Jan 
Date Detail:
Created Date:  2001-03-19     Completed Date:  2001-03-29     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  1273201     Medline TA:  Eur J Immunol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  186-95     Citation Subset:  IM    
Affiliation:
University of Rochester Medical Center, Rochester, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Antigen-Presenting Cells / physiology
Antigens, Neoplasm / chemistry,  immunology*
HSP70 Heat-Shock Proteins / chemistry,  immunology*
Heat-Shock Proteins / immunology*
Humans
Mice
Molecular Sequence Data
Phylogeny
T-Lymphocytes, Cytotoxic / immunology
Xenopus
Grant Support
ID/Acronym/Agency:
CA-44786/CA/NCI NIH HHS; CA-64394/CA/NCI NIH HHS; CA-76312/CA/NCI NIH HHS; R37 HD-07901/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, Neoplasm; 0/HSP70 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/sarcoma glycoprotein gp96 rejection antigens

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