| First Author | Tunnacliffe A | Year | 1989 |
| Journal | Int Immunol | Volume | 1 |
| Issue | 5 | Pages | 546-50 |
| PubMed ID | 2484963 | Mgi Jnum | J:249821 |
| Mgi Id | MGI:6100782 | Doi | 10.1093/intimm/1.5.546 |
| Citation | Tunnacliffe A, et al. (1989) The majority of human CD3 epitopes are conferred by the epsilon chain. Int Immunol 1(5):546-50 |
| abstractText | Transgenic mouse T cells expressing the human CD3 epsilon chain bind the majority (29/36) of monoclonal antibodies (mAbs) specific for human CD3. A proportion of these mAbs are also able to recognize isolated CD3 epsilon in a soluble, recombinant form. Thus, CD3 epsilon can confer most CD3 epitopes on the TCR--CD3 complex, but many determinants may require assembly of the complex for their formation. A number of mAbs did not recognize epsilon-transgenic T cells and probably need other CD3 subunits for binding. CD3-specific mAbs from each of the three groups defined here, as well as mAbs directed against the TCR alpha beta heterodimer, are all able to activate T cells. Therefore mAb attachment at several different sites on the TCR--CD3 complex can give rise to activation signals. This suggests that the cross-linking function of mitogenic antibodies may be their most significant property, rather than the perturbation of a particular 'functional epitope'. |
