A unique epitope on the CD2 molecule defined by the monoclonal antibody 9-1: epitope-specific modulation of the E-rosette receptor and effects on T-cell functions.

Monoclonal antibody (MoAb) 9-1 shows unique binding properties to CD2 resulting in peculiar epitope specific changes. 9-1 shows competitive binding with MoAb to D66 epitope, and gives a similar staining pattern with T-cell populations, at a low density on resting T cells, and high density on thymocytes and activated T cells. However, 9-1 has the opposite effect on anti-D66 MoAbs on rosette formation, namely, 9-1 increases the stability of rosettes, but 9-1 plus anti-mouse Ig bound to T-cell surface blocks rosettes. 9-1 plus anti-mouse Ig, like anti-D66 MoAbs, induces further appearance of D66 and 9-1 epitopes but, contrary to anti-D66, induces appearance of T11(3) epitopes. Thus, binding 9-1 results in unique "epitope-specific modulation" events that are not solely artificial, but appear to mimic events naturally occurring during T-cell differentiation/activation. The effects of binding 9-1 on T-cell functions also display peculiarities. 9-1, like anti-D66 MoAbs, activates T cells when added in combination with anti-9.6/T11(1) MoAbs but not with anti-T11(3). To obtain full activation, monocytes are required; however, adding 9-1 alone do not inhibit specific T-cell cytotoxicity contrary to anti-D66 or anti-9.6/T11(1), although 9-1 inhibits NK activity of peripheral cells. Given the apparent complexities of the functions exerted by CD2, these data show that definite conformational changes or reorientation, which would be naturally produced by soluble and/or cell surface ligand(s), would be key events in determining how CD2 will influence T-cell functions.