Characterization of T cell hybridomas raised against a glycopeptide containing the tumor-associated T antigen, (betaGal (1-3) alphaGalNAc-O/Ser) |
| |
Authors: | Gad Monika Werdelin Ole Meldal Morten Komba Shiro Jensen Teis |
| |
Institution: | (1) Institute for Medical Microbiology and Immunology, University of Copenhagen, Denmark;(2) The Carlsberg Laboratory, Department of Chemistry, Copenhagen, Denmark;(3) Pharmexa A/S, Hørsholm, Denmark |
| |
Abstract: | T cell hybridomas were raised against the glycopeptide S72 (Core-1) containing the tumor-associated disaccharide Gal (1–3) GalNAc (Core-1) O-linked to serine at position 72 in the mouse hemoglobin derived decapeptide Hb (67–76). All hybridomas recognized the glycopeptide S72 (Core-1). Two of the selected hybridomas responded, however, much better to the S72 (Tn) glycopeptide containing the monosaccharide GalNAc O-linked to serine. In addition, one hybridoma cross-responded to the glycopeptide T72 (Core-1) having a threonine at position 72 instead of a serine. No cross-responses were found to other glycopeptides consisting of the same hemoglobin peptide with different glycans attached or to the unglycosylated peptides. The T cell receptor V and V usage was clearly diverse. The CDR3 regions demonstrated moreover a predominance of small polar amino acid side chains, and three hybridomas contained a common sequence motif. All the sequenced CDR3 regions contained furthermore a conserved proline-glycine motif. In conclusion, immunization with the disaccharide containing glycopeptides S72 (Core-1) created a heterogeneous population of glycopeptide specific T cells with the ability of cross-responding toward related glycopeptides. |
| |
Keywords: | glycosylated tumor antigens T-antigen T cell hybridomas glycopeptide antigens Core-1 glycan |
本文献已被 PubMed SpringerLink 等数据库收录! |
|