Effect of single amino acid substitution at residue 167 of HLA-B51 on binding of antibodies and recognition of T cells

Hum Immunol. 1994 Mar;39(3):211-9. doi: 10.1016/0198-8859(94)90262-3.


We recently showed that a single amino acid substitution of tryptophane into glycine at residue 167 facing the "A pocket" forms a novel HLA-B51 subtype, B*5103, which is serologically discriminated as HLA-BTA. CDC assay of human alloantisera specific for the HLA-B5 CREG against B*5103- or B*5101-transfected human B-cell line, Hmy2C1R (C1R), supported the belief that human alloantisera can discriminate B*5103 from B*5101 Ag. Moreover, we found that 4D12 anti-B5, B35 CREG mAb cannot bind to B*5103 Ag on C1R cells or L cells although it binds to B*5101 Ag on both cells. These results indicate that alloantibodies can detect a single amino acid substitution at residue 167. Furthermore, it was suggested that 4D12 mAb recognizes the structure formed by the HLA-peptide complex since this mAb did not bind to empty HLA-B5, B35 CREG Ag on RMA-S transfectants. Six of eight anti-HLA-B*5101 CTL clones are not able to kill C1R cells expressing B*5103, indicating that conformational change of the A pocket by substitution at residue 167 has a crucial influence on recognition of alloreactive T cells. Therefore, discrimination of B*5103 from B*5101 would seem to be important in bone marrow transplantation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry*
  • Binding Sites, Antibody
  • Cell Line
  • Cytotoxicity Tests, Immunologic
  • HLA-B Antigens / chemistry*
  • HLA-B Antigens / immunology*
  • HLA-B35 Antigen / immunology
  • HLA-B51 Antigen
  • Humans
  • Isoantibodies / immunology
  • Molecular Sequence Data
  • Structure-Activity Relationship
  • T-Lymphocytes, Cytotoxic / immunology*
  • Transfection


  • Amino Acids
  • HLA-B Antigens
  • HLA-B35 Antigen
  • HLA-B51 Antigen
  • Isoantibodies