Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the beta chain

T Deufel, A Grove, Hans Kofod, A Lernmark

3 Citations (Scopus)

Abstract

Antibodies against synthetic peptides representing the class-II antigen HLA-DR and -DQ beta 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 beta 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.
Original languageEnglish
JournalF E B S Letters
Volume189
Issue number2
Pages (from-to)329-37
Number of pages9
ISSN0014-5793
Publication statusPublished - 23 Sept 1985

Keywords

  • Amino Acid Sequence
  • Animals
  • Antibodies
  • Cell Line
  • Cell Transformation, Viral
  • Enzyme-Linked Immunosorbent Assay
  • Flow Cytometry
  • Fluorescent Antibody Technique
  • HLA-DQ Antigens
  • HLA-DR Antigens
  • Herpesvirus 4, Human
  • Histocompatibility Antigens Class II
  • Lymphocytes
  • Rabbits

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