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According to the two-signal model of T cell activation, costimulatory molecules augment T cell receptor (TCR) signaling, whereas adhesion molecules enhance TCR-MHC-peptide recognition. The structure and binding properties of CD28 imply that it may perform both functions, blurring the distinction between adhesion and costimulatory molecules. Our results show that CD28 on naïve T cells does not support adhesion and has little or no capacity for directly enhancing TCR-MHC-peptide interactions. Instead of being dependent on costimulatory signaling, we propose that a key function of the immunological synapse is to generate a cellular microenvironment that favors the interactions of potent secondary signaling molecules, such as CD28.

Original publication




Journal article


Nature immunology

Publication Date





1159 - 1166


Department of Pathology and Immunology, Washington University School of Medicine, 660 S. Euclid Ave, St. Louis MO, USA.


T-Lymphocytes, Cells, Cultured, Cell Line, Jurkat Cells, Cell Membrane, Humans, Glycosylphosphatidylinositols, Intercellular Adhesion Molecule-1, Antigens, CD28, Recombinant Fusion Proteins, Antigens, CD80, Histocompatibility Antigens Class II, Lymphocyte Activation, Cell Adhesion, Protein Structure, Tertiary