Short synthetic glycopeptides successfully induce antibody responses to carcinoma-associated Tn antigen
| Autor: | Richard Lo-Man, Hiroshi Nakada, Claude Leclerc, Sophie Vichier-Guerre, Danièle Cantacuzene, Edith Dériaud, Sylvie Bay |
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| Rok vydání: | 2000 |
| Předmět: |
0303 health sciences
Antigenicity biology medicine.drug_class Chemistry Immunogenicity Tn antigen 010402 general chemistry Monoclonal antibody 01 natural sciences Biochemistry Molecular biology Epitope Glycopeptide 0104 chemical sciences 3. Good health 03 medical and health sciences Endocrinology Antigen medicine biology.protein Antibody 030304 developmental biology |
| Zdroj: | The Journal of Peptide Research. 55:173-180 |
| ISSN: | 1397-002X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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