Interactions of HLA-B27 with the peptide loading complex as revealed by heavy chain mutations

MHC class I heavy chains assemble in the endoplasmic reticulum with β2-microglobulin and peptide to form heterotrimers. Although full assembly is required for stable class I molecules to be expressed on the cell surface, class I alleles can differ significantly in their rates of, and dependencies on...

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Veröffentlicht in:International immunology 2001-10, Vol.13 (10), p.1275-1282
Hauptverfasser: Harris, Michael R., Lybarger, Lonnie, Myers, Nancy B., Hilbert, Christine, Solheim, Joyce C., Hansen, Ted H., Yu, Yik Y. L.
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container_end_page 1282
container_issue 10
container_start_page 1275
container_title International immunology
container_volume 13
creator Harris, Michael R.
Lybarger, Lonnie
Myers, Nancy B.
Hilbert, Christine
Solheim, Joyce C.
Hansen, Ted H.
Yu, Yik Y. L.
description MHC class I heavy chains assemble in the endoplasmic reticulum with β2-microglobulin and peptide to form heterotrimers. Although full assembly is required for stable class I molecules to be expressed on the cell surface, class I alleles can differ significantly in their rates of, and dependencies on, full assembly. Furthermore, these differences can account for class I allele-specific disparities in antigen presentation to T cells. Recent studies suggest that class I assembly is assisted by an elaborate complex of proteins in the endoplasmic reticulum, collectively referred to as the peptide loading complex. In this report we take a mutagenesis approach to define how HLA-B27 molecules interact with the peptide loading complex. Our results define subtle differences between how B27 mutants interact with tapasin (TPN) and calreticulin (CRT) in comparison to similar mutations in other mouse and human class I molecules. Furthermore, these disparate interactions seen among class I molecules allow us to propose a spatial model by which all class I molecules interact with TPN and CRT, two molecular chaperones implicated in facilitating the binding of high-affinity peptide ligands.
doi_str_mv 10.1093/intimm/13.10.1275
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Our results define subtle differences between how B27 mutants interact with tapasin (TPN) and calreticulin (CRT) in comparison to similar mutations in other mouse and human class I molecules. 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source MEDLINE; Oxford University Press Journals All Titles (1996-Current); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects antigen binding
Antiporters - metabolism
autoimmunity
Calcium-Binding Proteins - metabolism
Calreticulin
chaperones
CRT calreticulin
CXN calnexin
ER endoplasmic reticulum
etB27 epitope-tagged B27
HeLa Cells
histocompatibility antigen HLA
HLA-B27 Antigen - genetics
HLA-B27 Antigen - metabolism
Humans
immunochemistry
Immunoglobulins - metabolism
Membrane Transport Proteins
MHC
Models, Molecular
Molecular Chaperones - metabolism
Polysaccharides
Protein Binding
Protein Structure, Tertiary
Ribonucleoproteins - metabolism
TAP transporter associated with antigen processing
TPN tapasin
β2m β2-microglobulin
title Interactions of HLA-B27 with the peptide loading complex as revealed by heavy chain mutations
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