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  • Title: A mutant chaperone converts a wild-type protein into a tumor-specific antigen.
    Author: Schietinger A, Philip M, Yoshida BA, Azadi P, Liu H, Meredith SC, Schreiber H.
    Journal: Science; 2006 Oct 13; 314(5797):304-8. PubMed ID: 17038624.
    Abstract:
    Monoclonal antibodies have become important therapeutic agents against certain cancers. Many tumor-specific antigens are mutant proteins that are predominantly intracellular and thus not readily accessible to monoclonal antibodies. We found that a wild-type transmembrane protein could be transformed into a tumor-specific antigen. A somatic mutation in the chaperone gene Cosmc abolished function of a glycosyltransferase, disrupting O-glycan Core 1 synthesis and creating a tumor-specific glycopeptidic neo-epitope consisting of a monosaccharide and a specific wild-type protein sequence. This epitope induced a high-affinity, highly specific, syngeneic monoclonal antibody with antitumor activity. Such tumor-specific glycopeptidic neo-epitopes represent potential targets for monoclonal antibody therapy.
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