Abstract
THE CD4 and CDS molecules are transmembrane glycoproteins expressed by functionally distinct subsets of mature T cells. CD4+ and CD8+ T cells recognize antigens on major histocompatibility complex (MHC) class II-bearing and class I-bearing target cells respectively1–3. The ability of monoclonal antibodies against CD4 and CDS to block antigen recognition by T cells, as well as cell–cell adhesion assays4–7, indicate that CD4 and CDS bind to non-polymorphic determinants of class II or class I MHC. Here we demonstrate that soluble recombinant HLA-DR4 molecules from insect cells and HLA-DR-derived peptides bind to immobilized recombinant soluble CD4. CD4 binds recombinant soluble DR4 heterodimers, as well as the soluble DR4-β chain alone. Furthermore, two out of twelve DR4β peptides could interact specifically with CD4. These findings show that CD4 interacts with a region of MHC class II molecules analogous to a previously identified loop in class I MHC proteins that binds CDS (refs S, 9).
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Cammarota, G., Scheirle, A., Takacs, B. et al. Identification of a CD4 binding site on the β2 domain of HLA-DR molecules. Nature 356, 799–801 (1992). https://doi.org/10.1038/356799a0
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DOI: https://doi.org/10.1038/356799a0
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