All for CD91 and CD91 for all.
Heat shock proteins interact with antigen-presenting cells through their receptor, CD91, eliciting a cascade of events including maturation, activation and representation of chaperoned foreign peptides with class I molecules on their surface. In turn, this facilitates recognition of non-self leading to induction of a cytotoxic T cell response. The abundance of heat shock proteins in tumours and their presence in virion coats makes them attractive propositions for use in antitumour and antiviral strategies.
Stebbing
Justin
J
Department of Immunology, Division of Investigative Science, Faculty of Medicine, Imperial College of Science, Technology and Medicine, The Chelsea and Westminster Hospital, 369 Fulham Road, London SW10 9NH, UK. j.stebbing@imperial.ac.uk
Savage
Philip
P
Patterson
Steve
S
Gazzard
Brian
B
D000818:Animals; D000938:Antigen-Presenting Cells / Q000276:immunology; D015703:Antigens, CD / Q000276:immunology / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000276:immunology / Q000378:metabolism*; D018869:Heat-Shock Response / Q000276:immunology; D006801:Humans; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D018832:Molecular Chaperones / Q000276:immunology; D013602:T-Lymphocytes, Cytotoxic / Q000276:immunology
D015703:Antigens, CD; D006360:Heat-Shock Proteins; C475476:LRP1 protein, human; D026503:Low Density Lipoprotein Receptor-Related Protein-1; D018832:Molecular Chaperones