The H-2Kkml Mutation: A Single Nucleotide Substitution Causes Multiple Functional Differences in a Murine Class I MHC Molecule

  • J. M. Martinko
  • J. C. Solheim
  • J. Geliebter

Abstract

The polymorphic MHC class I glycoproteins are implicated in a number of immunologic reactions involving T-cell recognition. Among these polymorphic molecules in the murine H-2 complex, a number of mutants have been identified. One of these mutants was mapped to the H-2K k allele in the CBA inbred mouse strain and resulted in graft rejection and graft versus host reactions. This mutant was designated H-2K kml and the mouse strain carrying it was designated CBA.M523 (1). Analysis of the structural variation in the H-2K kml molecule identified a single nucleotide substitution at codon 152, resulting in a change from Asp (GAT) in Kk to Ala (GCT) in K kml (2). This report documents the completion of the nucleotide sequence coding for the extracellular domains of the altered K kml and compares the known K k coding sequence from the AKR strain (3) to that of the CBA strain which is ancestral to the CBA.M523 mutant-bearing strain.

Keywords

Cellulose Codon Recombination Glycine Oligomer 

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Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • J. M. Martinko
    • 1
  • J. C. Solheim
    • 1
  • J. Geliebter
    • 2
  1. 1.Department of MicrobiologySouthern Illinois UniversityCarbondaleUSA
  2. 2.The Rockefeller UniversityNew YorkUSA

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