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Science. 2006 Oct 13;314(5797):304-8.

A mutant chaperone converts a wild-type protein into a tumor-specific antigen.

Author information

  • 1Department of Pathology, Committee on Immunology, Committee on Cancer Biology, University of Chicago, Chicago, IL 60637, USA. aschieti@uchicago.edu

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.

PMID:
17038624
DOI:
10.1126/science.1129200
[PubMed - indexed for MEDLINE]
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