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© Research
Publication : The journal of peptide research : official journal of the American Peptide Society

Short synthetic glycopeptides successfully induce antibody responses to carcinoma-associated Tn antigen

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in The journal of peptide research : official journal of the American Peptide Society - 01 Feb 2000

Vichier-Guerre S, Lo-Man R, Bay S, Deriaud E, Nakada H, Leclerc C, Cantacuzène D

Link to Pubmed [PMID] – 10784033

J. Pept. Res. 2000 Feb;55(2):173-80

Glycopeptides containing a tumor-associated carbohydrate antigen (mono-, tri- or hexa-Tn antigen) as a B-cell epitope and a CD4+ T-cell epitope (PV: poliovirus or TT: tetanus toxin) were prepared for immunological studies. Several Tn antigen residues [FmocSer/Thr (alpha-GalNAc)-OH] were successively incorporated into the peptide sequence with unprotected carbohydrate groups. The tri- and hexa-Tn glycopeptides were recognized by MLS128, a Tn-specific monoclonal antibody. The position of the tri-Tn motif in the peptide sequence and the peptide backbone itself do not alter its antigenicity. As demonstrated by both ELISA and FACS analysis, the glycopeptides induced high titers of anti-Tn antibodies in mice, in the absence of a carrier molecule. In addition, the generated antibodies recognized the native Tn antigen on cancer cells. The antibody response obtained with a D-(Tn3)-PV glycopeptide containing three alpha-GalNAc-D-serine residues is similar that obtained with the Tn6-PV glycopeptide. These results demonstrate that short synthetic glycopeptides are able to induce anticancer antibody responses.