The first external domain of the nonobese diabetic mouse class II I-A beta chain is unique

Proc Natl Acad Sci U S A. 1987 Apr;84(8):2435-9. doi: 10.1073/pnas.84.8.2435.

Abstract

The nonobese diabetic mouse is recognized as an important animal model for human insulin-dependent diabetes mellitus. One of the components of susceptibility to this disease has been mapped to the major histocompatibility complex. In this study, full-length cDNA clones encoding the I-A alpha and beta chains from the nonobese diabetic mouse have been isolated and sequenced. They are identical to the sequences previously determined from the H-2d haplotype except for the sequence encoding the first external domain, the leader peptide, and the 5' untranslated region of the I-A beta chain molecule. Most strikingly, there are five consecutive nucleotide substitutions which lead to two radical amino acid changes in a region that is conserved between human and mouse. We suggest that the unique structure of the first external I-A beta chain domain is a major determinant in the disease susceptibility that maps to the major histocompatibility complex of the nonobese diabetic mouse.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA / analysis
  • Diabetes Mellitus, Experimental / immunology*
  • Genes, MHC Class II*
  • Histocompatibility Antigens Class II / analysis*
  • Macromolecular Substances
  • Major Histocompatibility Complex*
  • Mice
  • Mice, Inbred Strains
  • Mice, Mutant Strains
  • Polymorphism, Restriction Fragment Length
  • Species Specificity

Substances

  • Histocompatibility Antigens Class II
  • Macromolecular Substances
  • DNA

Associated data

  • GENBANK/M15848