CD4/major histocompatibility complex class II interaction analyzed with CD4‐ and lymphocyte activation gene‐3 (LAG‐3)‐Ig fusion proteins
- 1 September 1995
- journal article
- research article
- Published by Wiley in European Journal of Immunology
- Vol. 25 (9), 2718-2721
- https://doi.org/10.1002/eji.1830250949
Abstract
We analyzed CD4 major histocompatibility complex (MHC) class II interactions with CD4 and lymphocyte activation gene (LAG)-3 recombinant fusion proteins termed CD4Ig and LAG-3Ig. CD4Ig bound MHC class II molecules expressed on the cell surface only when used in the micromolar range. This weak CD4Ig binding was specific, since it was inhibited by anti-CD4 and anti-MHC class II mAb. LAG-3Ig bound MHC class II molecules with intermediate avidity (Kd = 60 nM at 37°C). Using LAG-3Ig as a competitor in a CD4/MHC class II-dependent cellular adhesion assay, we showed that this recombinant molecule was able to block CD4/MHC class II interaction. In contrast, no inhibition was observed in a CD4/MHC class II-dependent T cell cytotoxicity assay. Together, these results suggest that co-engagement of the TcR with CD4 alters the CD4/MHC class II molecular interaction to become insensitive to LAG-3Ig competition.Keywords
This publication has 29 references indexed in Scilit:
- Lymphocyte‐activation gene 3/major histocompatibility complex class II interaction modulates the antigenic response of CD4+ T lymphocytesEuropean Journal of Immunology, 1994
- Amino acid residues that flank core peptide epitopes and the extracellular domains of CD4 modulate differential signaling through the T cell receptor.The Journal of Experimental Medicine, 1994
- A rationally designed CD4 analogue inhibits experimental allergic encephalomyelitisNature, 1994
- Mouse CD4 binds MHC class II with extremely low affinityInternational Immunology, 1993
- Identification of a CD4 binding site on the β2 domain of HLA-DR moleculesNature, 1992
- Death of mature T cells by separate ligation of CD4 and the T-cell receptor for antigenNature, 1990
- Activated CD8 binding to class I protein mediated by the T-cell receptor results in signallingNature, 1990
- The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domainCell, 1989
- Possible involvement of the T4 molecule in T cell recognition of class II HLA antigens. Evidence from studies of CTL-target cell binding.The Journal of Experimental Medicine, 1984
- The major histocompatibility complex-restricted antigen receptor on T cells. II. Role of the L3T4 product.The Journal of Experimental Medicine, 1983