Biochemical differences in Qa-2 antigens expressed by Qa-2+,6+ and Qa-2+,6- strains. Evidence for differential expression of the Q7 and Q9 genes

Abstract

Cell surface forms of Qa-6 class I molecules are biochemically indistinguishable from Qa-2 although Qa-6 maps telomeric to Qa-2 with the recombinant strain B6.K2. Analysis of appropriate F1 strains did not demonstrate the presence of a trans acting factor that could modify the Qa-2 molecule to produce the Qa-6 determinant. Also, neither a neighboring cell surface molecule nor oligosaccharides were found to block the recognition of the Qa-6 determinant in Qa-2+,6- strains. The 2-D gel profiles of neuraminidase or endoglycosidase treated anti-Qa-2 immunoprecipitates from lysates of cell surface iodinated Qa-2+,6+ strains revealed an additional basic polypeptide which was absent from that of Qa-2+,6- strains. Thus, differential sialylation/glycosylation of Qa-2 molecules masks detection of Qa-2 antigen heterogeneity when cell surface forms are analyzed. Qa-6+ phenotype associated polypeptides were also found at various stages of post-translational processing in cells metabolically labeled in the presence and absence of tunicamycin. Northern analyses using Q7 and Q9 specific oligonucleotide probes revealed appropriate sized transcripts for both genes in the Qa-2+,6+ strain B6 but only Q9 in the Qa-2+,6- strain B6.K2. These data demonstrate that there is structural heterogeneity in Qa-2 antigens expressed by Qa-2+,6+ and Qa-2+,6- strains which results from differential expression of the Q7 and Q9 genes.