HLA-DP genotyping with sequence-specific oligonucleotides can detected known sequence variations in the polymorphic segments of the DPB1 second exon. Since the allelic polymorphism of the 22 published alleles is based on recombination of sequence motifs from six variable regions, DPB1 typing depends on the reactivity pattern of many different probes rather than from typing with single allele-specific probes. By computer simulation, we have previously shown that the minimal set of probes to define the 22 different alleles and most of the heterozygous combinations is 18. Here we describe HLA-DPB1 typing results and allele frequencies in a panel of 200 unrelated Caucasians from Southwest Germany. The result confirmed the power of the new HLA-DPB1 typing method, but we failed to detect three of the previously described alleles in our panel. To accommodate with the observed 19 different alleles, the sequence and hybridization conditions of 17 oligonucleotide probes are given, which are able to differentiate all except two, resolved by group-specific amplification, of the 190 possible heterozygous phenotypes.
The molecular reaction patterns of the DRw52-specific mouse monoclonal antibodies UL-52 and 7.3.19.1 were investigated. Upon immunoprecipitation and two-dimensional IEF-SDS polyacrylamide gel electrophoresis analysis (2D-PAGE) mAb UL-52 selectively isolated DR beta 1 molecules from DRw52-positive cell lines, whereas mAb 7.3.19.1 predominantly precipitated DR beta 3 molecules. Reduced mAb UL-52 binding affinity was observed to DRw8- and DRw12-positive cells, potentially resulting from structural modifications within the antibody binding site. Comparison of mAb UL-52 reactivity with published DR beta chain amino acid sequences demonstrates that the amino acid residues -S- in positions 11 and 13 on DR beta 1 molecules essentially contribute to the formation of the antibody binding site. mAb 7.3.19.1 reactivity, on the other hand, correlates with the expression of DR beta 3 chain amino acid residues K, G and N, in positions 71, 73 and 77, respectively. In contrast to other DRw52 monoclonal antibodies described so far, mAb UL-52 demonstrates a similar reactivity to DRw52 allosera, suggesting that mAb UL-52 and DRw52 allosera possibly recognize the same or a similar determinant on DR beta 1 molecules.
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