The Leukocyte Immunoglobulin-Like Receptor Family Member LILRB5 Binds to HLA-Class I Heavy Chains

The Leukocyte Immunoglobulin-Like Receptor Family Member LILRB5 Binds to HLA-Class I Heavy Chains

The leukocyte immunoglobulin-like receptor (LILR) family includes inhibitory and stimulatory members which bind to classical and non-classical HLA-class I. The ligands for many LILR including LILRB5 have not yet been identified. We generated C-terminal eGFP and N-terminal FLAG-tagged fusion construc...

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Bibliographic Details
Published in:PloS one 2015-06, Vol.10 (6), p.e0129063-e0129063
Main Authors: Zhang, Zhiyong, Hatano, Hiroko, Shaw, Jacqueline, Olde Nordkamp, Marloes, Jiang, Guosheng, Li, Demin, Kollnberger, Simon
Format: Article
Language:eng
Subjects:
Animals
Antigens, CD - metabolism
Antisera
Arthritis
B7 antigen
Binding
Cell Line
Cell lines
Chains
Dimers
Histocompatibility antigen HLA
HLA-B27 Antigen - metabolism
HLA-B7 Antigen - metabolism
Humans
Identification methods
Immunoglobulins
Immunology
Immunoprecipitation
Laboratories
Leukocytes
Ligands
Monocytes
Peptides
Protein Binding
Proteins
Rats
Receptors, Immunologic - metabolism
Rheumatology
White blood cells
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Summary:The leukocyte immunoglobulin-like receptor (LILR) family includes inhibitory and stimulatory members which bind to classical and non-classical HLA-class I. The ligands for many LILR including LILRB5 have not yet been identified. We generated C-terminal eGFP and N-terminal FLAG-tagged fusion constructs for monitoring LILR expression. We screened for LILR binding to HLA-class I by tetramer staining of 293T cells transfected with LILRA1, A4, A5 A6 and LILRB2 and LILRB5. We also studied HLA class I tetramer binding to LILRB5 on peripheral monocyte cells. LILRB5 binding to HLA-class I heavy chains was confirmed by co-immunoprecipitation. HLA-B27 (B27) free heavy chain (FHC) dimer but not other HLA-class I stained LILRB5-transfected 293T cells. B27 dimer binding to LILRB5 was blocked with the class I heavy chain antibody HC10 and anti-LILRB5 antisera. B27 dimers also bound to LILRB5 on peripheral monocytes. HLA-B7 and B27 heavy chains co-immunoprecipitated with LILRB5 in transduced B and rat basophil RBL cell lines. Our findings show that class I free heavy chains are ligands for LILRB5. The unique binding specificity of LILRB5 for HLA-class I heavy chains probably results from differences in the D1 and D2 immunoglobulin-like binding domains which are distinct from other LILR which bind to β2m-associated HLA-class I.
ISSN:1932-6203
1932-6203