A trans-acting major histocompatibility complex-linked gene whose alleles determine gain and loss changes in the antigenic structure of a classical class I molecule

• Published in: The Journal of experimental medicine Vol. 170; no. 3; pp. 777 - 795
• Main Authors: Livingstone, A M, Powis, S J, Diamond, A G, Butcher, G W, Howard, J C
• Format: Journal Article
• Language: English
• Published: New York, NY Rockefeller University Press 01.09.1989; The Rockefeller University Press
• Subjects: Alleles; Animals; Antigens; Biological and medical sciences; Chromosome Mapping; Epitopes - analysis; Female; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Histocompatibility antigens (hla, h-2 and other systems); Histocompatibility Antigens Class I - analysis; Histocompatibility Antigens Class I - biosynthesis; Major Histocompatibility Complex; Male; Molecular immunology; Peptide Mapping; Polysaccharides - analysis; Rats; T-Lymphocytes, Cytotoxic; Rat; Molecular structure; Cytotoxicity test; Major histocompatibility system; Rodentia; Monoclonal antibody; Peptide map; Vertebrata; Immunogenetics; Immunoprecipitation reaction; Regulation(control); Mammalia; Alloantigen; Gene; Class I histocompatibility antigen
• ISSN: 0022-1007; 1540-9538
• DOI: 10.1084/jem.170.3.777

The RT1.A locus of the rat MHC encodes the H chain of the single classical class I molecule of this species. One of the alleles of this polymorphic locus, RT1.Aa, is present in several laboratory inbred, congenic, and MHC recombinant rat strains. Studies of the RT1.Aa class I molecule from a number of these strains as a target for CTL show that its antigenicity, both as an alloantigen and a restricting element, is subject to gain and loss alterations by the action of a gene mapping in the MHC to the right of RT1.A. This locus is apparently present in two allelic forms (one possibly a null allele) corresponding to the presence or absence of a dominant transacting modifier, and has been named class I modification, or cim. The antigenic change brought about by cim is scarcely detectable serologically but highly immunogenic for CTL. Biochemical investigations show that cim affects the post-translational modification of RT1.Aa.