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Recognition of a Sequestered Self Peptide by Influenza Virus-Specific CD8⁺ Cytolytic T Lymphocytes¹

Rong Fan^2,*,, Scott S. Tykodi^2,*,§ and Thomas J. Braciale^3,*,,

^* Beirne B. Carter Center for Immunology Research and Departments of Microbiology and Pathology, University of Virginia Health Sciences Center, Charlottesville, VA 22908; and ^§ Division of Biology and Biomedical Science, Immunology Program, Washington University School of Medicine, St. Louis, MO 63110

The Ag receptors on CD8⁺ CTL recognize foreign antigenic peptides associated with cell surface MHC class I molecules. Peptides derived from self proteins are also normally presented by MHC class I molecules. Here we report that an H-2K^d-restricted murine CD8⁺ CTL clone directed to an influenza hemagglutinin epitope can recognize a peptide derived from the murine mitochondrial aconitase enzyme in association with H-2K^d molecules. Surprisingly, this self peptide is not normally displayed on the cell surface associated with the restricting MHC class I molecule. Several lines of evidence suggest that this self peptide, although requiring association with the K^d molecule for CTL recognition, is not associated with this or other MHC class I allele under physiologic conditions in intact cells. Rather, it is sequestered in the cytoplasm associated with a carrier protein and is released only upon cell disruption. These results suggest a means of restricting the entry of self peptide into the class I pathway. In addition, this finding raises the possibility that self peptides sequestered within the cell can, after release from damaged cells, interact with MHC class I molecules on bystander cells and trigger autoimmune injury by virus-specific CTLs during viral infection.

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