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The Journal of Immunology, 2001, 167: 5543-5547.
Copyright © 2001 by The American Association of Immunologists


Cutting Edge

Cutting Edge: Leukocyte Receptor Complex-Encoded Immunomodulatory Receptors Show Differing Specificity for Alternative HLA-B27 Structures1

Rachel L. Allen2,*, Tim Raine*, Anja Haude*, John Trowsdale* and Michael J. Wilson*,{dagger}

* Department of Pathology, University of Cambridge, Cambridge, United Kingdom; and {dagger} Discovery Research, GlaxoSmithKline, Stevenage, United Kingdom

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.




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