The majority of human CD3 epitopes are conferred by the epsilon chain.

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Tunnacliffe A, Olsson C, de la Hera A

The majority of human CD3 epitopes are conferred by the epsilon chain.

Int Immunol. 1989;1(5):546-50. doi: 10.1093/intimm/1.5.546.

PubMed ID

2484963 [ View in PubMed

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Abstract

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'.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Mosunetuzumab	T-cell surface glycoprotein CD3 epsilon chain	Protein	Humans	Yes	Binder	Details