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Conformation of the T‐Cell Antigen Receptor‐β Chain C‐Domain Contributes to Vβ 3 Epitope Recognition by Monoclonal Antibody KJ25
Author(s) -
LI ZHANGUO,
KEMP O.,
LONGHURST T.,
MANOLIOS N.
Publication year - 1996
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1046/j.1365-3083.1996.d01-21.x
Subject(s) - epitope , t cell receptor , monoclonal antibody , microbiology and biotechnology , antigen , alpha chain , antibody , recombinant dna , linear epitope , chemistry , t cell , beta (programming language) , biology , receptor , biochemistry , immune system , gene , immunology , computer science , programming language
The clonotypic T‐cell antigen receptor (TCR)‐β chain contains two extracellular intrachain disulfide bonds. It belongs to the immunoglobulin gene superfamily and is subdivided into variable (V), joining (J), diversity (D) and constant (C) region. Monoclonal antibody (MoAb) KJ25 is believed to recognize an epitope in the V‐domain of TCR‐β (Vβ 3 ) chain, but its epitope requirements are unknown. In this study of TCR‐αβ chain interactions using chimeric recombinant TCR‐β chains, the authors found that partial substitution of the Cβ‐domain with that of interleukin‐2 receptor α chain (Tac) sequences led to the loss of TCR‐Vβ 3 epitope recognition by KJ25. These results suggest that epitope recognition of the TCR‐Vβ 3 by KJ25 MoAb is dependent not only on the V‐domain, but also on the close contact with the extracellular C‐domain which influences the conformation and epitope recognition of the Vβ 3 ‐region. This may not be unique to Vβ 3 and may be a general feature of TCR‐β protein folding.