Distinguishing self from nonself: immunogenicity of the murine H47 locus is determined by a single amino acid substitution in an unusual peptide.
Document Type
Article
Publication Date
2001
Keywords
Amino-Acid-Sequence, Autoantigens, Cell-Line, Isoleucine, Membrane-Proteins, Mice-Inbred-BALB-C, Mice-Inbred-C57BL, Minor-Histocompatibility-Antigens, Molecular-Sequence-Data, Mutagenesis-Site-Directed, Oligopeptides, Peptide-Fragments, Phenylalanine, Polymorphism-(Genetics), Protein-Binding
First Page
4438
Last Page
4445
JAX Source
J Immunol 2001 Apr; 166(7):4438-45.
Abstract
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 D(b) 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.
Recommended Citation
Mendoza LM,
Villaflor G,
Eden P,
Roopenian D,
Shastri N.
Distinguishing self from nonself: immunogenicity of the murine H47 locus is determined by a single amino acid substitution in an unusual peptide. J Immunol 2001 Apr; 166(7):4438-45.