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ReportsA Mutant Chaperone Converts a Wild-Type Protein into a Tumor-Specific Antigen
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.
1 Department of Pathology, Committee on Immunology, Committee on Cancer Biology, University of Chicago, Chicago, IL 60637, USA. * These authors contributed equally to this work.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)
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