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Locus‐specific detection of HLA‐DQ and ‐DR antigens by antibodies against synthetic N‐terminal octapeptides of the β chain
Author(s) -
Deufel Thomas,
Grove Anne,
Kofod Hans,
Lernmark Åke
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81050-4
Subject(s) - antiserum , microbiology and biotechnology , antigen , antibody , immunofluorescence , peptide , gel electrophoresis , biology , chemistry , biochemistry , immunology
Antibodies against synthetic peptides representing the class‐II antigen HLA‐DR and ‐DQ β chain N‐terminal sequences were prepared in rabbits. The two octapeptides only share two amino acids and enzyme‐linked immuno‐assays showed the antisera only to bind to its own antigen. Both peptide antisera detected a 29 kDa component in immunoblots of Raji and AL‐34 cell plasma membrane proteins separated by SDS gel electrophoresis. The binding of either N‐terminal peptide antiserum was selectively inhibited only by the peptide used as antigen. Indirect immunofluorescence.analysis by flow cytofluorometry showed specific surface immunofluorescence in 1:100–1:1000 dilutions in lymphoblastoid and blood mononucleated cells. In the latter the binding was primarily confined to monocytes and a subpopulation of lymphocytes. It is concluded that locus‐specific immunological reagents to distinguish between β chains of HLA‐DR and ‐DQ have been prepared by the preparation by the production of antibodies against the N‐terminal sequences of each polypeptide