Recent studies have shown that cytotoxic T lymphocytes form conjugates with antigen-negative targets.' These studies have further demonstrated that this process of antigen-independent conjugate formation (AIC) is mediated by way of two adhesion pathways: one involving the T cell-CD2 receptor binding to the ligand LFA-3* on the target, and the other involving the T cell-LFA-I receptor interacting with ICAM-1 and probably other ligandsj on the target. While the roles of CD2, LFA-I , and LFA-3 in CTL-mediated lysis (CML) have been demonstrated a b ~ n d a n t l y , ~ very little is known about the role of ICAM-I in such lysis. ICAM-I was initially proposed as a ligand for LFA-I , based upon monoclonal antibody (mAb) inhibition of LFA-1-dependent T-cell adhesion to fibroblasts and the finding that inhibition occurred with pretreatment of the fibroblasts and not the T cell.5.h These findings have been extended to and confirmed in AIC using CTL c1ones.j We initially investigated the role of ICAM-I by mAb-inhibition studies of AIC formation, and showed that its utilization in LFAI-dependent conjugates varied significantly between target^,^ irrespective of the ICAM1 level expressed on the target. To analyze its role in CML, targets that predominantly used ICAM-I in AIC were selected. One such target is U937 (a prornonocytic line).3 The ability of the ICAM-1 mAb to inhibit antigen-independent, phorbol myristic acetate (PMA)/ ionophore-triggered lysis of U937 by a CTL clone was studied. The results in FIGURE 1A showed that ICAM-1 mAb inhibits lysis by 70%; lysis is also inhibited well by the LFA-1 mAb (go%), and to a limited extent by CD2 (27%) and LFA-3 (38%) mAb. Following this result, a bulk population of allospecific T cells were prepared by two cycles of in vitro stimulation of peripheral blood mononuclear leukocytes with irradiated U937 as stimulator cells. The bulk population was tested in a standard C M L assay. The result in FIGURE 1B showed 75% inhibition by the ICAM-1 mAb, compared with 95%, 2096, and 15% inhibition by LFA-I , CD2, and LFA-3 mAb, respectively. These results showed that ICAM-I is critical for antigen-specific C T L recognition in this effectoritarget combination. Studies with various effectoritarget combinations revealed differing utilization and requirements for ICAM-1 in C T L r e ~ o g n i t i o n . ~ The results are consistent with the interpretation that ICAM-I can serve as one ligand for LFA-I in CTL recognition. The role of ICAM-1 in CTL recognition correlates closely with its ability to inhibit
[1]
T. Springer,et al.
Functional evidence that intercellular adhesion molecule‐1 (icam‐1) is a ligand for lfa‐1d‐ependent adhesion in t cell‐mediated cytotoxicity
,
1988,
European journal of immunology.
[2]
Michael Loran Dustin,et al.
The T lymphocyte glycoprotein CD2 binds the cell surface ligand LFA-3
,
1987,
Nature.
[3]
T. Springer,et al.
Two antigen-independent adhesion pathways used by human cytotoxic T-cell clones
,
1986,
Nature.
[4]
Michael Loran Dustin,et al.
A human intercellular adhesion molecule (ICAM-1) distinct from LFA-1.
,
1986,
Journal of immunology.
[5]
Michael Loran Dustin,et al.
Induction by IL 1 and interferon-gamma: tissue distribution, biochemistry, and function of a natural adherence molecule (ICAM-1).
,
1986,
Journal of immunology.
[6]
J. Strominger,et al.
Three distinct antigens associated with human T-lymphocyte-mediated cytolysis: LFA-1, LFA-2, and LFA-3.
,
1982,
Proceedings of the National Academy of Sciences of the United States of America.