Abstract
Molecular chaperones, also known as heat-shock proteins or HSPs, are a functionally conserved class of proteins whose primary function is to keep cellular proteins in their native conformation, under both physiological and stress conditions. In most cases these chaperones do not participate in the final mature structures that their ‘clients’ form. Apart from folding, chaperones play vital roles in cellular localization, transport, secretion and assembly of proteins in multiprotein complexes
Highlights
Molecular chaperones, known as heat-shock proteins or HSPs, are a functionally conserved class of proteins whose primary function is to keep cellular proteins in their native conformation, under both physiological and stress conditions
As tumour cells were shown to be completely reliant on chaperones for their survival, attempts to inhibit chaperones, HSP90, using pharmacologic and nonpharmacologic means were made with encouraging results
Experiments demonstrated that purified members of HSP70 and HSP90 family could be used as tumour specific vaccine which can elicit tumour rejection, a property largely dependent on the tumour cells ‘peptidome’ binding ability of these chaperones
Summary
Known as heat-shock proteins or HSPs, are a functionally conserved class of proteins whose primary function is to keep cellular proteins in their native conformation, under both physiological and stress conditions. There is a strong need for a highly specific and non-toxic adjuvant therapy for GBM patients. Two properties of HSPs make them suitable for eliciting anti-tumour immune response, (1) they bind to misfolded antigenic peptides with high-affinity providing a snapshot or fingerprint of a tissue/cell and (2) antigen presenting cells have evolved to see HSPs as danger signals and have unique receptors that make them readily internalizable and induce a strong cytotoxic T cell response [8,9].
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