The major histocompatibility complex (MHC) class I molecules expressed at the cell surface are associated with a large number of different peptides so that the density of a given MHC-peptide complex is relatively low. Here we describe the properties of MHC class I molecules genetically attached to a single antigenic peptide. Cells expressing these fusion proteins are recognized by T cells specific for the particular MHC-peptide complex. Coculture of naive splenocytes with cells expressing these MHC-peptide fusion proteins and the B7.1 antigen allows the induction of primary cytotoxic T lymphocytes (CTL) in vitro. Injection of these cells into naive mice enhances the frequency of specific CTL precursors and protects against a subsequent challenge with a tumor or a virus bearing the antigenic peptide. Soluble MHC-peptide fusions were also produced in which all three components, that is, the heavy chain, beta 2-microglobulin and the peptide, have fused into a single-chain protein. The availability of MHC class I molecules bound to a single peptide provides valuable tools for the manipulation of CTL responses and the analysis of the selection processes in the thymus.
Cells expressing a major histocompatibility complex class I molecule with a single covalently bound peptide are highly immunogenic.
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E Mottez, P Langlade-Demoyen, H Gournier, F Martinon, J Maryanski, P Kourilsky, J P Abastado; Cells expressing a major histocompatibility complex class I molecule with a single covalently bound peptide are highly immunogenic.. J Exp Med 1 February 1995; 181 (2): 493–502. doi: https://doi.org/10.1084/jem.181.2.493
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