DR5-associated DC molecules carry three different allospecificities

• Published in: Human immunology Vol. 12; no. 1; p. 47
• Main Authors: Tanigaki, N, Tosi, R, Centis, D, Ferrara, G B
• Format: Journal Article
• Language: English
• Published: United States 01-01-1985
• Subjects: Antibody Specificity; Family; Female; Histocompatibility Antigens Class II - immunology; HLA-DR5 Antigen; Humans; Isoantibodies - genetics; Isoantibodies - immunology; Male; Phenotype; Population Surveillance; Radioimmunoassay
• ISSN: 0198-8859
• DOI: 10.1016/0198-8859(85)90253-8

Antiserum 8w670 which had been classified as anti-DR5 in the Workshop analysis was found by the direct binding test to react with about 40% of Ia molecules in an Ia preparation from LG38 cells (DR5,5) that was deleted of DR molecules and DR-like molecules we call BR and enriched in DC molecules by pretreatment with a rabbit antiserum raised against alpha-subunits of DR and BR molecules. The specificity involved in the binding reaction was shown by the binding inhibition assay to be present in 100% of DR5-positive cases (53 out of 53) and 8w13-positive cases (2 out of 2) and in 23% of DR4-positive cases (4 out of 17). This association pattern did not correspond to any of the known supertypic specificities including the DC beta 4 and DC alpha 3, both of which had been found on DR5-associated DC molecules. Yet sequential binding analysis revealed that the 8w670-defined specificity was indeed present on the same molecules carrying DC beta 4 and DC alpha 3 specificities. This specificity was designated DC5.