Abstract
Successful interaction of a T cell with antigen (AG) requires, besides a T-cell receptor (TCR), the expression of a number of coreceptor molecules which provide the binding (formation) of the AGMHC protein complex (MHC - main histocompatibility complex) and signal transduction into the cell [8]. Specifically, AG-specific activation involves an adhesive molecule LFA-I (lymphocyte function-associated antigen) which is not directly bound to TC1L This molecule belongs to the family of integrins, heterodimers with non-covalently bound o~- and B-chains. These transmembrane proteins are associated with the cytoplasmic domains of the cytoskeleton. By interacting with the ligand ICAM-I (intercellular adhesion molecule), LFA-I provides an additional adhesive mechanism necessary to the cell for implementing some other interactions such as MHC/AG-receptor, TCR, cytokines, etc. [6]. It is known that in vitro antibodies to LFA-I a-chain suppress a proliferative response in a mixed culture of lymphocytes (MCL) [9], Tcell proliferation in response to phytohemagglutinin (PHA) [4], concanavalin A, production of interleukin-2, and the T-cell-mediated antibody response [13], and also inhibit the lytic function of
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