Immunotherapy for human cancer using heat shock protein-peptide complexes
Author:
Publisher
Springer Science and Business Media LLC
Subject
Oncology
Link
http://link.springer.com/content/pdf/10.1007/s11912-005-0035-8.pdf
Reference36 articles.
1. Srivastava P: Interaction of heat shock proteins with peptides and antigen presenting cells: chaperoning of the innate and adaptive immune responses. Annu Rev Immunol 2002, 20:395–425.
2. Srivastava PK, Udono H, Blachere NE, Li Z: Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics 1994, 39:93–98.
3. Zhu X, Zhao X, Burkholder WF, et al.: Structural analysis of substrate binding by the molecular chaperone DnaK. Science 1996, 272:1606–1614.
4. MacAry PA, Javid B, Floto RA, et al.: HSP70 peptide binding mutants separate antigen delivery from dendritic cell stimulation. Immunity 2004, 20:95–106. The authors identify the minimal domain of mycobacterial hsp70 necessary for peptide binding and for antigen re-presentation by APCs. A mutation of a key amino acid in the peptide-binding domain abrogates re-presentation activity but not stimulation of chemokine and cytokine release by dendritic cells. The re-presentation activity of hsp70 is shown to be calcium dependent.
5. Gidalevitz T, Biswas C, Ding H, et al.: Identification of the N-terminal peptide binding site of glucose-regulated protein 94. J Biol Chem 2004, 279:16543–16552. Using molecular modeling and mutational analysis, this study identifies a peptide-binding site in the N-terminal domain of gp96 and discusses in a comparative manner some attributes of peptidebinding clefts of MHC I, hsp70, and gp96.
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