Open AccessLupus‐derived autoantibodies with dual autoactivity: anti‐DNA and anti‐Fc. II. Fine specificity of anti‐self autoreactivity
Author(s) -
RUMBLEY C. A.,
VOSS E. W.
Publication year - 1995
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1995.tb03788.x
Subject(s) - autoantibody , epitope , isotype , immunology , antibody , antigen , monoclonal antibody , monoclonal , immunoglobulin g , subclass , microbiology and biotechnology , biology , chemistry
SUMMARY The anti‐immunoglobulin reactivity of two monoclonal, dual specific, autoantibodies, BV 17–45 and BV 04‐01 was examined. The current study further defined the anti‐immunoglobulin autoreactivity of these MoAbs to be Fc‐specific. Both BV 17–45 and BV 04‐01 bound their own Fc domains in addition to Fc regions of other MoAbs of similar isotype with varying levels of activity. The different anti‐Fc reactivity patterns of BV 17–45 and BV 04‐01 suggested that these MoAbs recognized distinct epitopes. Neither BV 17–45 nor BV 04‐01 bound Fab fragments or single‐chain antibody derivatives, which confirmed that the anti‐immunoglobulin reactivity of these autoantibodies was Fc‐specific. In addition, abrogation of anti‐Fc reactivity was observed when affinity‐labelled MoAbs were used as coating antigens in solid‐phase ELISAs. These results implied that active‐site ligand binding induced cotiformational changes which altered the Fc epitope(s) recognized by BV 17–45 and BV 04‐01.