Journal
SCIENCE
Volume 314, Issue 5797, Pages 304-308Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1129200
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Funding
- NCI NIH HHS [P01-CA97296, R01-CA22677, R01-CA37516] Funding Source: Medline
- NCRR NIH HHS [P41RR018502-01] Funding Source: Medline
- NICHD NIH HHS [HD 07009] Funding Source: Medline
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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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