| First Author | Mendoza LM | Year | 2001 |
| Journal | J Immunol | Volume | 166 |
| Issue | 7 | Pages | 4438-45 |
| PubMed ID | 11254699 | Mgi Jnum | J:74957 |
| Mgi Id | MGI:2159492 | Doi | 10.4049/jimmunol.166.7.4438 |
| Citation | Mendoza LM, et al. (2001) Distinguishing self from nonself: immunogenicity of the murine H47 locus is determined by a single amino acid substitution in an unusual peptide. J Immunol 166(7):4438-45 |
| abstractText | 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. |
