Monoclonal antibody against murine T cell receptor V alpha 14 cross-reacts with human CD3 epsilon and detects disulfide-linked dimeric form. |
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Authors: | T Ito K Ishibashi K Imai H Koseki C S Ra E Fernandez M Kantake T Saito M Taniguchi |
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Affiliation: | Division of Molecular Immunology, School of Medicine, Chiba University, Japan. |
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Abstract: | A monoclonal antibody against V14+ alpha-chain of murine T cell receptor (TCR) was established by fusing spleen cells from a rat immunized with a soluble chimeric TCR/IgG3 protein containing murine TCR V alpha 14J alpha 281 in place of the VHDHJH of an IgG3. lambda 1, and subjected to screening on a human transfectant (Jurkat variant) expressing the murine V14J281 alpha-chain. The anti-mouse V alpha 14 antibody precipitated TCR alpha beta molecules from Triton X-100-solubilized extracts of 125I-labeled murine thymocytes and spleen cells. Unexpectedly, the antibody showed cross-reactivity to the human CD3 epsilon molecule and detected a disulfide-linked 20 kDa dimeric form of human CD3 epsilon, which is a novel family component of the CD3 complex and is associated closely with the CD3 zeta-zeta homodimer as well as TCR alpha beta or TCR gamma delta. |
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Keywords: | CD3 /math/theta.gif" ALT=" {theta}" BORDER=" 0" > disulfide-linked dimer TCR-CD3 complex anti-mouse V /math/alpha.gif" ALT=" {alpha}" BORDER=" 0" >14 |
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