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The Journal of Immunology, 2000, 164: 4627-4634.
Copyright © 2000 by The American Association of Immunologists

Functional and Phenotypic Evidence for Presentation of E{alpha}52–68 Structurally Related Self-Peptide(s) in I-E{alpha}-Deficient Mice1

Christophe Viret and Charles A. Janeway, Jr.2

Section of Immunobiology and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510

The Y-Ae mAb and the 1H3.1 TCR-{alpha}ß (V{alpha}1/Vß6) are two immune receptors specific for I-Ab MHC class II molecules complexed to the 52–68 fragment of the {alpha}-chain of I-E class II molecules (the E{alpha}52–68 peptide). A profound intrathymic negative selection occurs in 1H3.1 TCR transgenic mice in the presence of an I-E{alpha} transgene. The administration of mAbs to 1H3.1/I-E{alpha} double-transgenic newborn mice reveals that Y-Ae, but not the isotype-matched anti-I-E Y17 mAb, rescues a significant number of mature (Vß6highCD4+CD8-) thymocytes and allows the detection of E{alpha}52–68-reactive T cells in the periphery. These observations indicate that deletion of autoreactive T cells can be specifically inhibited in vivo by an mAb specific for the deleting self-peptide:self-MHC class II complex. Similar inhibition experiments indicate that C57BL/6 (I-Ab+/I-E{alpha}-) mice constitutively express an E{alpha}-independent, Y-Ae-recognizable epitope(s). This finding is confirmed by the phenotypic analysis of mature (MHC class II high) C57BL/6 bone marrow-derived dendritic cells. Collectively, these observations further illustrate the peptide specificity of negative selection and demonstrate that MHC class II-positive cells from unmanipulated C57BL/6 mice that lack a functional I-E{alpha} gene can assemble one or more self-peptide:I-Ab complexes recognizable by the E{alpha}52–68:I-Ab complex-specific Y-Ae mAb.







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