Mutation at amino acid position 133 of H-2D(d) prevents β2m association and immune recognition but not surface expression

Ronald J. Rubocki, Janet M. Connolly, Ted H. Hansen*, Roger W. Melvold, Byung S. Kim, William H. Hildebrand, John Martinko

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

The histocompatibility loss mutation H-2(dm6) was derived from a mouse treated with the chemical mutagen ethylnitrosourea, and previous mapping studies implicated D(d) as the affected locus. Southern blot analyses of DNA from H-2(dm6) cells did not detect major deletions in the D(dm6) gene, suggesting that H-2(dm6) was different from the previously characterized D region mutants H-2(dm1) and H-2(dm2). RNA blot analysis identified D(dm6) transcripts of appropriate size and a D(dm6) protein was immunoprecipitated from biosynthetically labeled H-2(dm6) cells. Interestingly, the D(dm6) protein showed no β2m association and was only precipitated by a mAb to the α3 domain. Furthermore, oligosaccharide maturation and low levels of surface expression of D(dm6) molecules were detected. However, the surface D(dm6) was nonfunctional as a target Ag in in vitro cytotoxicity assays, consistent with its original in vivo detection as a loss mutation. Sequence analyses of D(dm6) cDNA identified a single nucleotide base difference from wild-type, resulting in the substitution of a Trp to Arg at position 133. The significance of this substitution is discussed in the context of other class I expression variants.

Original languageEnglish (US)
Pages (from-to)2352-2357
Number of pages6
JournalJournal of Immunology
Volume146
Issue number7
StatePublished - 1991

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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