Sep 1, 1989

Status of an unpaired thiol group on the HLA-B27 epitope

Clinical and Experimental Immunology
L McLeanJ R Archer


Sequence analysis and site-directed mutagenesis of HLA-B27 indicate an unpaired cysteine at position 67 of the hypervariable region corresponding to its serologically defined, disease-associated epitope. We investigated whether chemical modification of this thiol group affected the serological reactions of B27. B27-positive cells were treated with thiol-blocking agents and then tested for recognizable B27 expression. Anti-HLA-B27 alloantisera and monoclonal antibodies were used in cytotoxicity, absorption, and cellular ELISA (cELISA). The semi-quantitative cytotoxicity-based assays showed some decrease in both B27 and controls. However, cELISA indicated that the inhibition of B27 was significantly greater than control antigens, and dependent on thiol-blocker concentration. This suggests that a proportion of HLA-B27 molecules have a free, reactive thiol at the antibody-defined epitope. Incomplete inhibition by thiol-blocking agents indicates that the remainder are inaccessible.

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Mentioned in this Paper

Monoclonal Antibodies
Antigenic Specificity
Sulfhydryl Compounds
Sulfhydryl Reagents
HLA Class I Histocompatibility Antigen, B-27 alpha Chain
Nongranular Leukocyte
Enzyme-Linked Immunosorbent Assay
Cysteine Hydrochloride

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