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International Immunology
Year: 2010  |  Volume: 22  |  Issue: 4  |  Page No.: 299 - 306

The recognition of {gamma}{delta} TCR to protein antigen does not depend on the hydrophobic I97 residue of CDR3{delta}

X Xi, L Cui and W. He    

Abstract:

The crystal structure analysis demonstrated that the hydrophobic amino acid residue (isolecuine/leucine/valine) at conserved position 97 of V2 TCR plays an important role in recognizing the non-peptide antigen. But its importance to protein antigen remains unclear until now. In the present study, we focus on the role of hydrophobic amino acid residue at conserved position 97 of V2 TCR in complementarity determining region (CDR)3-mediated binding to protein antigen. We employed CDR3 peptide and membrane-engineered TCR as detecting molecules with mutated 97 hydrophobic amino acid residue in CDR3 (nominated as OT10), a V2 CDR3 sequence derived from tumor infiltrating lymphocytes in ovarian epithelial carcinoma (OEC). Binding assays revealed that OT10 peptide and membrane-engineered TCR ( TCR transfected cells with OT10 sequence) could bind specifically ovarian tumor cell line (SKOV3). The mutant analysis indicated that any amino acid substitution at position I97 could abolish the response of the transfected cells to iso-butylamine, a known non-peptide antigen of T cells. But amino acid substitution of isoleucine at position 97 did not change the responsiveness of TCR transfected cell to protein antigen. Our data suggested that a mechanism other than non-peptide antigen might mediate the recognition of V2 T cells for protein antigen. This finding may provide a possibility that TCR recognize different ligands in diversity manners.

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