Leukocyte receptor complex-encoded immunomodulatory receptors show differing specificity for alternative HLA-B27 structures

J Immunol. 2001 Nov 15;167(10):5543-7. doi: 10.4049/jimmunol.167.10.5543.

Abstract

We studied recognition of the disease-associated HLA-B27 allele by immunomodulatory receptors encoded within the leukocyte receptor complex. HLA class I are ligands for members of the killer Ig receptor (KIR) and Ig-like transcript (ILT)/LIR/LILR families (the new LILR nomenclature is described at www. gene.ucl.ac.uk/nomenclature/genefamily/lilr.html). Members of these families bound HLA-B27 in both classical and beta(2) microglobulin-independent forms. Classical complexes bound ILT2, ILT4, and LIR6 transfectants but not ILT1, ILT3, or ILT5. A free H chain form of HLA-B27 bound ILT4 and LIR6. Both forms of HLA-B27 bound KIR3DL1 transfectants. HLA-B27 free H chain bound CD14(+) cells in PBL from healthy controls, consistent with ILT4 expression on monocytes. Alternative recognition of different forms of HLA-B27 by KIR or ILT could influence their immunomodulatory function and may imply a role in inflammatory disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, CD / genetics
  • Antigens, CD / metabolism
  • Cell Line
  • Cells, Cultured
  • HLA-B27 Antigen / chemistry*
  • HLA-B27 Antigen / metabolism*
  • Humans
  • Leukocyte Immunoglobulin-like Receptor B1
  • Lymphocytes / immunology
  • Membrane Glycoproteins
  • Receptors, Immunologic / genetics
  • Receptors, Immunologic / metabolism*
  • Receptors, KIR
  • Receptors, KIR3DL1
  • Transfection

Substances

  • Antigens, CD
  • HLA-B27 Antigen
  • KIR3DL1 protein, human
  • LILRA2 protein, human
  • LILRB1 protein, human
  • LILRB2 protein, human
  • Leukocyte Immunoglobulin-like Receptor B1
  • Membrane Glycoproteins
  • Receptors, Immunologic
  • Receptors, KIR
  • Receptors, KIR3DL1
  • leukocyte-immunoglobulin--like receptor 6