Abstract
The spondylitis associated HLA-B27 epitope includes a characteristic unpaired cysteine at amino acid position 67. On some B27 molecules the thiol (-SH) side chain of this residue seems to be available for chemical interactions. The possibility that free radicals produced during inflammation might specifically affect this group was investigated in this work. Cells bearing HLA-B27 were exposed to free radicals generated by ultraviolet irradiation or hydrogen peroxide, and HLA antigens were then measured by flow cytometry. Binding of monoclonal antibodies to B27 was not affected. These results do not support a specific susceptibility of HLA-B27 to damage by free radicals, despite its apparently vulnerable structure.
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Selected References
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- Allan I. M., Lunec J., Salmon M., Bacon P. A. Reactive oxygen species selectively deplete normal T lymphocytes via a hydroxyl radical dependent mechanism. Scand J Immunol. 1987 Jul;26(1):47–53. doi: 10.1111/j.1365-3083.1987.tb02233.x. [DOI] [PubMed] [Google Scholar]
- Lunec J., Blake D. R., McCleary S. J., Brailsford S., Bacon P. A. Self-perpetuating mechanisms of immunoglobulin G aggregation in rheumatoid inflammation. J Clin Invest. 1985 Dec;76(6):2084–2090. doi: 10.1172/JCI112212. [DOI] [PMC free article] [PubMed] [Google Scholar]
- MacLean L., Macey M., Lowdell M., Badakere S., Whelan M., Perrett D., Archer J. Sulphydryl reactivity of the HLA-B27 epitope: accessibility of the free cysteine studied by flow cytometry. Ann Rheum Dis. 1992 Apr;51(4):456–460. doi: 10.1136/ard.51.4.456. [DOI] [PMC free article] [PubMed] [Google Scholar]
- el-Zaatari F. A., Sams K. C., Taurog J. D. In vitro mutagenesis of HLA-B27. Amino acid substitutions at position 67 disrupt anti-B27 monoclonal antibody binding in direct relation to the size of the substituted side chain. J Immunol. 1990 Feb 15;144(4):1512–1517. [PubMed] [Google Scholar]