Re-evaluating the role of heat-shock protein-peptide interactions in tumour immunity.
Early investigations into the immune surveillance of chemically-induced sarcomas led to two important concepts in tumour immunobiology: one, tumour rejection can be elicited by immune recognition of tumour antigens; and two, tumours express unique sets of antigens, which are known as tumour-specific antigens. The pioneering studies of Srivastava and colleagues led to the proposal that heat-shock proteins (HSPs) function as ubiquitous tumour-specific antigens, with the specificity residing in a population of bound peptides that identify the tissue of origin of the HSP. However, recent findings, including new data on the cell biology of peptide generation and trafficking, have called into question the specificity of tumour rejection that is induced by HSPs.
Nicchitta
Christopher V
CV
Department of Cell Biology, Duke University Medical Centre, Durham, North Carolina 27710, USA. c.nicchitta@cellbio.duke.edu
D000818:Animals; D000951:Antigens, Neoplasm / Q000276:immunology / Q000502:physiology; D006360:Heat-Shock Proteins / Q000502:physiology*; D051379:Mice; D018448:Models, Immunological; D009374:Neoplasms, Experimental / Q000276:immunology*; D010455:Peptides / Q000276:immunology
D000951:Antigens, Neoplasm; D006360:Heat-Shock Proteins; D010455:Peptides; C052646:sarcoma glycoprotein gp96 rejection antigens