Mutation at amino acid position 133 of H-2Dd 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

24 Scopus citations

Abstract

The histocompatibility loss mutation H-2dm6 was derived from a mouse treated with the chemical mutagen ethylnitrosourea, and previous mapping studies implicated Dd as the affected locus. Southern blot analyses of DNA from H-2dm6 cells did not detect major deletions in the Ddm6 gene, suggesting that H-2dm6 was different from the previously characterized D region mutants H-2dm1 and H-2dm2. RNA blot analysis identified Ddm6 transcripts of appropriate size and a Ddm6 protein was immunoprecipitated from biosynthetically labeled H-2dm6 cells. Interestingly, the Ddm6 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 Ddm6 molecules were detected. However, the surface Ddm6 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 Ddm6 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 - Apr 1 1991

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint

Dive into the research topics of 'Mutation at amino acid position 133 of H-2Dd prevents β2m association and immune recognition but not surface expression'. Together they form a unique fingerprint.

Cite this