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The Journal of Immunology, 2001, 166: 4438-4445.
Copyright © 2001 by The American Association of Immunologists

Distinguishing Self from Nonself: Immunogenicity of the Murine H47 Locus Is Determined by a Single Amino Acid Substitution in an Unusual Peptide1

Lisa M. Mendoza*, Gilbert Villaflor*, Peter Eden2,{dagger}, Derry Roopenian{dagger} and Nilabh Shastri3,*

* Division of Immunology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720; and {dagger} The Jackson Laboratory, Bar Harbor, ME 04609

Histocompatibility (H) Ags are responsible for chronic graft rejection and graft vs host disease in solid tissue and bone marrow transplantation among MHC-matched individuals. Here we defined the molecular basis of self-nonself discrimination for the murine chromosome 7 encoded H47 histocompatibility locus, known by its trait of graft-rejection for over 40 years. H47 encodes a novel, highly conserved cell surface protein containing the SCILLYIVI (SII9) nonapeptide in its transmembrane region. The p7 isoleucine-to-phenylalanine substitution in SII9 defined the antigenic polymorphism and T cell specificity. Despite absence of the canonical consensus motif and weak binding to Db MHC I, both H47 peptides were presented to CTLs. However, unlike all the other known H loci, the relative immunogenicity of both H47 alleles varied dramatically and was profoundly influenced by neighboring H loci. The results provide insights into the peptide universe that defines nonself and the basis of histoincompatibility.




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