Overlapping but Nonidentical Binding Sites on CD2 for CD58 and a Second Ligand CD59
- 26 June 1992
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 256 (5065), 1805-1807
- https://doi.org/10.1126/science.1377404
Abstract
The interaction of the T cell glycoprotein CD2 with one ligand, CD58, contributes to T cell function. We have identified CD59, a glycoprotein with complement-inhibitory function, as a second physiological ligand for CD2. Antibodies to CD59 inhibit CD2-dependent T cell activation in murine T cell hybridomas expressing human CD2. In an in vitro binding assay with purified CD58 and CD59, CD2+ cells bind not only immobilized CD58 but also CD59. With two complementary approaches, it was demonstrated that the binding sites on CD2 for CD58 and CD59 are overlapping but nonidentical. These observations suggest that direct interactions between CD2 and both CD58 and CD59 contribute to T cell activation and adhesion.Keywords
This publication has 31 references indexed in Scilit:
- GPI-Anchored Cell-Surface Molecules Complexed to Protein Tyrosine KinasesScience, 1991
- The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2–6 sialyltransferase, CD75, on B cellsCell, 1991
- Binding of the integrin Mac-1 (CD11b/CD18) to the third immunoglobulin-like domain of ICAM-1 (CD54) and its regulation by glycosylationCell, 1991
- LFA-3, CD44, and CD45: Physiologic Triggers of Human Monocyte TNF and IL-1 ReleaseScience, 1990
- Adhesion receptors of the immune systemNature, 1990
- H19, a surface membrane molecule involved in T-cell activation, inhibits channel formation by human complementCellular Immunology, 1990
- 20 KDa homologous restriction factor of complement resembles T cell activating proteinBiochemical and Biophysical Research Communications, 1989
- Isolation and characterization of a membrane protein from normal human erythrocytes that inhibits reactive lysis of the erythrocytes of paroxysmal nocturnal hemoglobinuria.Journal of Clinical Investigation, 1989
- The Biologic Roles of CD2, CD4, and CD8 in T-Cell ActivationAnnual Review of Immunology, 1989
- Two antigen-independent adhesion pathways used by human cytotoxic T-cell clonesNature, 1986