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Shared structural motifs in TCR of glycopeptide‐recognizing T cell hybridomas

The TCR structure of T cell hybridomas recognizing a tumor glycan‐defined epitope has been studied using reverse transcriptase‐PCR and gene sequencing. The hybridomas had been raised against a glycopeptide, T72(Tn), consisting of the mouse hemoglobin‐derived decapeptide Hb(67 – 76), O‐glycoslated in position 72 with α‐D‐GalNAc. The glycan‐specific hybridomas varied widely in their use of Vα genes although Vα4 was predominant, being present in one third of them. The Vβ gene usage was more restricted and dominated by Vβ1 and Vβ15. There was no correlation between Vα and Vβ usage and antigen fine specificity of the hybridomas. The overall amino acid composition of the complementarity‐determining region (CDR) 3 of the hybridomas was dominated by small polar residues such as Gly, Asn, Ser, Glu and Ala, amino acids reported in the literature to be frequent in glycan‐recognizing proteins. Furthermore, the CDR3 of most hybridomas also contained an aromatic residue with preference for Tyr. A few of the hybridomas raised against the T72(Tn) glycopeptide were peptide specific, i.  e. they responded to the unglycosylated peptide only. The amino acid usage of their CDR3 regions was not radically different from that of the glycopeptide specific hybridomas. They also preferentially used Vα4. However, Vβ4 and Vβ8 were the dominating β chains.