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International Immunology, Vol. 14, No. 7, pp. 775-782, July 2002
© 2002 Japanese Society for Immunology

The assembly of functional ß2-microglobulin-free MHC class I molecules that interact with peptides and CD8+ T lymphocytes

Todd D. Schell1, Lawrence M. Mylin1,3, Satvir S. Tevethia1 and Sebastian Joyce2

1 Department of Microbiology and Immunology, Pennsylvania State University, College of Medicine, Hershey, PA 17033, USA 2 Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA 3 Present address: Messiah College, Grantham, PA 17027, USA

Correspondence to: S. Joyce; E-mail: sebastian.joyce{at}vanderbilt.edu
Transmitting editor: L. L. Lanier

Functional MHC class I molecules are expressed on the cell surface in the absence ofß2-microglobulin (ß2m) light chain that can interact with CD8+ T lymphocytes. Whether their assembly requires peptide binding and whether their recognition by CD8+ T lymphocytes involves the presentation of peptide epitopes remains unknown. We show that ß2m-free H-2Db assembles with short peptides that are ~9 amino acid residues in length, akin to ligands associated with completely assembled ß2m+ H-2Db. Remarkably, a subset of the peptides associated with the ß2m-free H-2Db has an altered anchor motif. However, they also include peptides that contain a ß2m+H-2Db binding anchor motif. Further, the H-2Kb- and H-2Db-restricted peptide epitopes derived from SV-40 T antigen also assemble with H-2b class I in ß2m-deficient cells and are recognized by epitope-specific CD8+ T lymphocytes. Taken together our data reveal that functional MHC class I molecules assemble in the absence of ß2m with peptides and form CD8+ T lymphocyte epitopes.

Keywords: ß2-microglobulin, antigen processing and presentation, CD8+ T lymphocytes, MHC class I, SV-40 T antigen epitope


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