Cell-surface expression and immune receptor recognition of HLA-B27 homodimers.

Cell-surface expression and immune receptor recognition of HLA-B27 homodimers.

OBJECTIVE: HLA-B27 is capable of forming in vitro a heavy-chain homodimer structure lacking beta(2)-microglobulin. We undertook this study to ascertain if patients with spondylarthritis express beta(2)-microglobulin-free HLA-B27 heavy chains in the form of homodimers and receptors for HLA-B27 homod...

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Xehetasun bibliografikoak
Egile Nagusiak:	Kollnberger, S, Bird, L, Sun, M, Retiere, C, Braud, V, McMichael, A, Bowness, P
Formatua:	Journal article
Hizkuntza:	English
Argitaratua:	2002

Antzeko izenburuak

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Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling.
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HLA-B27 heavy chain homodimers are expressed in HLA-B27 transgenic rodent models of spondyloarthritis and are ligands for paired Ig-like receptors.
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CELL SURFACE EXPRESSION OF HLA B27 HEAVY CHAINS AND SPECIFIC RECOGNITION BY IMMUNE RECEPTORS, POSSIBLE ROLE IN SPONDYLOARTHROPATHY
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TARGETING MONOCYTE-EXPRESSED HLA-B27 HOMODIMERS IN ANKYLOSING SPONDYLITIS
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Inhibiting HLA-B27 homodimer-driven immune cell inflammation in spondylarthritis.
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HLA-B-27 heavy chain homodimer formation and natural killer cell family interaction - comparison of two HLA-B-27 subtypes in vitro
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Interaction of HLA-B27 homodimers with KIR3DL1 and KIR3DL2, unlike HLA-B27 heterotrimers, is independent of the sequence of bound peptide.
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Th17 cells expressing KIR3DL2+ and responsive to HLA-B27 homodimers are increased in ankylosing spondylitis.
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Dimers are forever. Expression and recognition of abnormal HLA-B27 in spondylo arthritis
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HLA B27 can form heavy chain homodimers in vivo and in vivo, possible role of cys 67.
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HLA-B27-Homodimer-Specific Antibody Modulates the Expansion of Pro-Inflammatory T-Cells in HLA-B27 Transgenic Rats.
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Functional characterisation of HLA-B27 in autoimmunity
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HLA-B27 homodimers differ in their interactions with LILRB1, LILRB2, KIR3DL1 and KIR3DL2 compared to HLA-B27 heterotrimers
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HLA-B*2709, A SUBTYPE NOT ASSOCIATED WITH ANKYLOSING SPONDYLITIS, FORMS FEWER HOMODIMERS THAN HLA-B*2705
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Cutting edge: HLA-B27 can form a novel beta 2-microglobulin-free heavy chain homodimer structure.
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EXPRESSION OF HLA-B27 HEAVY CHAIN FORMS IN ANKYLOSING SPONDYLITIS AND HLA-B27 POSITIVE CELL LINES
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The KIRs of HLA-B27: the role of HLA-B27 KIR interactions in infection and spondyloarthritis
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Residue Cys-67 of HLA-B27 contributes to antigen presentation and T cell recognition of HLA-B27 restricted T cell epitopes.
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The role of B27 heavy chain dimer immune receptor interactions in spondyloarthritis.
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The role of HLA-B27 interactions with natural killer receptors in the pathogenesis of spondyloarthritis
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The solvent-inaccessible Cys67 residue of HLA-B27 contributes to T cell recognition of HLA-B27/peptide complexes.
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The role of HLA-B27 in spondyloarthritis.
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Factors determining the cell surface expression of a novel HLA-B27 epitope
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HLA-B27 HEAVY CHAIN DIMER EXPRESSION IN SPONDYLOARTHRITIS
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HLA-B27
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HLA-B27: natural function and pathogenic role in spondyloarthritis.
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Expression of aberrant HLA-B27 molecules is dependent on B27 dosage and peptide supply.
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Direct visualisation of HLA-B27 forms in cell lines and Spondyloarthropathy tissues
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THE ARTHRITIS-ASSOCIATED HLA-B(star)27:05 FORMS MORE CELL SURFACE B27 DIMER AND FREE HEAVY CHAIN LIGANDS FOR KIR3DL2 AND LILRB2 IMMUNORECEPTORS THAN HLA(star)B27:09
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Molecular Characterisation Of The Killer Cell Immunoglobulin-Like Receptor 3DL2 Binding To Aberrant HLA-B27 Heavy Chains In Spondyloarthritis
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