NDLI: Characterization of an immunodominant cancer-specific O-glycopeptide epitope in murine podoplanin (OTS8)

Content Provider	Springer Nature Link
Author	Steentoft, Catharina Schjoldager, Katrine T. Cló, Emilia Mandel, Ulla Levery, Steven B. Pedersen, Johannes W. Jensen, Knud Blixt, Ola Clausen, Henrik
Copyright Year	2010
Abstract	Auto-antibodies induced by cancer represent promising sensitive biomarkers and probes to identify immunotherapeutic targets without immunological tolerance. Surprisingly few epitopes for such auto-antibodies have been identified to date. Recently, a cancer-specific syngeneic murine monoclonal antibody 237, developed to a spontaneous murine fibrosarcoma, was shown to be directed to murine podoplanin (OTS8) with truncated Tn O-glycans. Our understanding of such cancer-specific auto-antibodies to truncated glycoforms of glycoproteins is limited. Here we have investigated immunogenicity of a chemoenzymatically produced Tn-glycopeptide derived from the putative murine podoplanin O-glycopeptide epitope. We found that the Tn O-glycopeptide was highly immunogenic in mice and produced a Tn-glycoform specific response with no reactivity against unglycosylated peptides or the O-glycopeptide with extended O-glycan (STn and T glycoforms). The immunodominant epitope was strictly dependent on the peptide sequence, required Tn at a specific single Thr residue (Thr77), and antibodies to the epitope were not found in naive mice. We further tested a Tn O-glycopeptide library derived from human podoplanin by microarray analysis and demonstrated that the epitope was not conserved in man. We also tested human cancer sera for potential auto-antibodies to similar epitopes, but did not detect such antibodies to the Tn-library of podoplanin. The reagents and methods developed will be valuable for further studies of the nature and timing of induction of auto-antibodies to distinct O-glycopeptide epitopes induced by cancer. The results demonstrate that truncated O-glycopeptides constitute highly distinct antibody epitopes with great potential as targets for biomarkers and immunotherapeutics.
Starting Page	571
Ending Page	582
Page Count	12
File Format	PDF
ISSN	02820080
Journal	Glycoconjugate Journal
Volume Number	27
Issue Number	6
e-ISSN	15734986
Language	English
Publisher	Springer US
Publisher Date	2010-08-19
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Autoantibody O-glycosylation O-glycopeptide Podoplanin Pathology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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