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Åke Lernmark

Principal investigator

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Site-specific antibodies distinguish single amino acid substitutions in position 57 in HLA-DQ β-chain alleles associated with insulin-dependent diabetes


  • D. Atar
  • T. Dyrberg
  • B. Michelsen
  • A. Karlsen
  • H. Kofod
  • J. Molvig
  • A. Lernmark

Summary, in English

The HLA-DQ β-chain gene shows a close association with susceptibility or resistance to autoimmune insulin-dependent diabetes mellitus (IDDM) and it has been suggested that the amino acid in position 57 may be of pathogenetic importance. To study the expression of the IDDM associated HLA-DQ β-chain alleles, we immunized rabbits with 12 to 13 amino acid long peptides representing HLA-DQw7 and -DQw8 allelic sequences, differing only by one amino acid in position 57 being aspartic acid (Asp) and alanine (Ala), respectively. Immunoblot analysis of lymphoblastoid cells showed that several antisera recognized a 29-kDa protein, equivalent to the expected molecular size of the HLA-DQ β-chain to yield two antisera for HLA-DQw7 (pos. 57(Asp)) and three antisera for HLA-DQw8 (pos. 57(Ala)) positive cells. Analysis of HLA-DR 3/4 positive IDDM patients (n = 24) and controls (n = 19) showed that all (100%) patients were positive for pos. 57(Ala) antiserum compared to 13 of 19 (68%) of the controls. The remaining six controls reacted with the pos. 57(Asp) antisera, whereas none of the patients did. We have therefore successfully been able to generate site-specific antibodies that distinguish single amino acid substitutions in predetermined positions of allelic HLA-DQ β-chain gene products. Such sera should become useful to detect and investigate HLA associated susceptibility to autoimmune diseases in man.

Publishing year







Journal of Immunology





Document type

Journal article


American Association of Immunologists


  • Endocrinology and Diabetes
  • Medical Genetics




  • ISSN: 0022-1767