Abstract
The T cell receptor (TCR) comprises an antigen-specific αβ heterodimer non-covalently associated with the CD3 γδε{lunate} and TCR ζ subunits. Both the CD3 and TCR ζ subunits are proposed to be responsible for the intracellular signal-transduction events. We report here the production of eight monoclonal antibodies (mAbs) that bind in an ELISA assay to a 113 amino acid synthetic peptide corresponding to the cytoplasmic domain of TCR ζ. Western blot analysis of anti-CD8 precipitates of lysates of transfectants expressing chimeric CD8/ζ constructs encoding increasing COOH-terminal truncations of TCR ζ indicates that four of these mAbs recognized the region of TCR ζ chain comprising the last 29 COOH-terminal residues. Thus, this region of TCR ζ may encode an immunodominant epitope. Furthermore, one of these mAbs, G3, is capable of precipitating both non-phosphorylated and tyrosine phosphorylated TCR ζ. The G3 mAb should be useful for elucidiating the structural and signalling characteristics of the TCR ζ chain.
Original language | English (US) |
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Pages (from-to) | 261-268 |
Number of pages | 8 |
Journal | Journal of Immunological Methods |
Volume | 170 |
Issue number | 2 |
DOIs | |
State | Published - Apr 15 1994 |
Keywords
- Epitope mapping
- Monoclonal antibody
- T cell receptor ζ chain
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology