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Peptide-Specific Intercellular Transfer of MHC Class II to CD4⁺ T Cells Directly from the Immunological Synapse upon Cellular Dissociation¹

Scott A. Wetzel^2,*, Timothy W. McKeithan and David C. Parker^3,*

^* Department of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, OR 97239; and Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198

The transfer of membrane proteins from APC to T cells was initially described in the 1970s, and subsequent work has described two mechanisms of transfer: APC-derived exosomes and direct transfer of small packets, while cells remain conjugated. Using fibroblast APC expressing a GFP-tagged I-E^k molecule with covalently attached antigenic peptide, we observed a third mechanism in live cell imaging: T cells spontaneously dissociating from APC often capture MHC:peptide complexes directly from the immunological synapse. Using two I-E^k-restricted murine TCR transgenic T cells with different peptide specificity, we show in this study that the MHC transfer is peptide specific. Using blocking Abs, we found that MHC:peptide transfer in this system requires direct TCR-MHC:peptide interactions and is augmented by costimulation through CD28-CD80 interactions. Capture of the GFP-tagged MHC:peptide complexes correlates with an activated phenotype of the T cell, elevated CD69 with down-modulated TCR. The transferred MHC:peptide molecules transferred to the T cell are associated with molecules that imply continued TCR signaling; p56^lck, phosphotyrosine, and polarization of the actin cytoskeleton.

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