Inhibition of T cell activation and adhesion functions by soluble CD2 protein.

Abstract:

:The CD2 (T11) molecule belongs to a family of cell-surface glycoproteins that function as adhesion molecules in the immune system. Human CD2 is found exclusively on cells of the T lineage: peripheral T lymphocytes, NK cells, and thymocytes. CD2 binds specifically to the surface glycoprotein LFA-3. CD2/LFA-3 adhesion is the basis for the formation of rosettes between T cells and sheep erythrocytes (SRBC) which bear the sheep homologue of LFA-3. More importantly, CD2/LFA-3 adhesion functions in the immune system to augment T cell activation; it initiates conjugate formation between participating T cells and antigen-presenting cells (APC). We investigated the effects of soluble forms of CD2 (sCD2), produced in either baculovirus or CHO expression systems, on the rosetting of T cells with SRBC and on the activation of T cells by antigen plus major histocompatibility complex (MHC) molecules. Rosette formation between T cells and SRBC was completely inhibited by as little as 1 microM sCD2. Furthermore, sCD2 effectively inhibited (at micromolar concentrations) the T cell proliferative response to recall antigens including rubella, tetanus toxoid, and herpes simplex virus (HSV-1), as well as alloantigens in a mixed lymphocyte culture. These findings are consistent with the notion that the CD2/LFA-3 interaction augments antigen-specific T cell functions. The use of a CD2 "decoy" molecule rather than anti-CD2 or anti-LFA-3 antibodies to block the CD2/LFA-3 interaction rules out secondary antibody effects, via the Fc portion, as the basis for inhibition of T cell activation and directly stresses the importance of this adhesion interaction in T cell responses.

journal_name

Cell Immunol

journal_title

Cellular immunology

authors

Rabin EM,Gordon K,Knoppers MH,Luther MA,Neidhardt EA,Flynn JF,Sardonini CA,Sampo TM,Concino MF,Recny MA

doi

10.1006/cimm.1993.1133

subject

Has Abstract,Author List Incomplete

pub_date

1993-06-01 00:00:00

pages

24-38

issue

1

eissn

0008-8749

issn

1090-2163

pii

S0008874983711330

journal_volume

149

pub_type

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