Importance of a conserved TCR J alpha-encoded tyrosine for T cell recognition of an HLA B27/peptide complex.

Importance of a conserved TCR J alpha-encoded tyrosine for T cell recognition of an HLA B27/peptide complex.

Human HLA B27-restricted cytotoxic T lymphocytes (CTL) specific for the influenza A epitope NP383-391 use similar TCR alpha and beta chains, with two closely related J alpha segments used by six of nine CTL clones from three unrelated donors (Bowness et al., Eur J. Immunol. 1993. 23: 1417-1421). The...

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Bibliografiske detaljer
Main Authors:	Bowness, P, Allen, R, Barclay, D, Jones, E, Mcmichael, A
Format:	Journal article
Sprog:	English
Udgivet:	1998

Lignende værker

Identification of T cell receptor recognition residues for a viral peptide presented by HLA B27.
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IDENTIFICATION OF T-CELL RECEPTOR RECOGNITION RESIDUES FOR AN INFLUENZA-VIRUS NONAMER PEPTIDE EPITOPE PRESENTED BY HLA B27
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The role of HLA-B27 in spondyloarthritis.
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HLA-B27-RESTRICTED PEPTIDE PRESENTATION TO CYTOTOXIC T-CELLS IN REACTIVE ARTHRITIS
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Fully functional HLA B27-restricted CD4+ as well as CD8+ T cell responses in TCR transgenic mice.
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Dimers are forever. Expression and recognition of abnormal HLA-B27 in spondylo arthritis
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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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HLA-B27
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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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Udgivet: (1998)

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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Interrogating the recognition landscape of a conserved HIV-specific TCR reveals distinct bacterial peptide cross-reactivity
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Interrogating the recognition landscape of a conserved HIV-specific TCR reveals distinct bacterial peptide cross-reactivity
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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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HLA B27 in health and disease: a double-edged sword?
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Lymphoblastoid cells express HLA-B27 homodimers both intracellularly and at the cell surface following endosomal recycling.
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