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Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cell lines

Saleki, K.; Hartigan, N.; van Lith, M.; Bulleid, N.; Benham, A.M.

Authors

K. Saleki

N. Hartigan

M. van Lith

N. Bulleid



Abstract

MHC class I molecules are predominantly involved in the presentation of antigens from viral proteins to CD8+ T cells of the immune system. However, MHC proteins can also be linked to autoimmune diseases, and the HLA-B27 allele is expressed by 95% of people with the rheumatic condition ankylosing spondylitis (AS). A precise molecular explanation for the association between HLA-B27 and AS is still lacking, although it is known that inappropriately disulfide bonded HLA-B27 heavy chains can be found at both the cell surface and in the endoplasmic reticulum (ER) of HLA-B27 expressing cells. This papers shows that HLA-B27 heavy chain misfolding does not depend on any unpaired cysteine residue per se when HLA-B27 is highly expressed. Also shown is that major differences exist in the disulfide-dependent conformations of two HLA-B27 subtypes, HLA-B2704 and HLA-B2705. The results imply that residues 77, 152, and/or 211 influence the redox potential of the MHC class I heavy chain and suggest that manipulating the redox environment can alter the conformational state of HLA-B27 subtypes.

Citation

Saleki, K., Hartigan, N., van Lith, M., Bulleid, N., & Benham, A. (2006). Differential oxidation of HLA-B2704 and HLA-B2705 in lymphoblastoid and transfected adherent cell lines. Antioxidants and Redox Signaling, 8(3-4), 292-299. https://doi.org/10.1089/ars.2006.8.292

Journal Article Type Article
Publication Date 2006-03
Journal Antioxidants and Redox Signaling
Print ISSN 1523-0864
Electronic ISSN 1557-7716
Publisher Mary Ann Liebert
Peer Reviewed Peer Reviewed
Volume 8
Issue 3-4
Pages 292-299
DOI https://doi.org/10.1089/ars.2006.8.292