Abstract
The structures recognized by monoclonal anti-IgG1 rheumatoid factors (RF) were localized by testing their reactivity with mutant immunoglobulins carrying gamma 1 chains that lacked either the CH1 or the CH3 domains. While optimal binding was observed in the absence of CH1, deletion of CH3 completely abolished the reactivity of all but one of the 71 monoclonal RF tested. Similar experiments were carried out with IgG2a- and IgG2b-specific RF by using variant immunoglobulins carrying various hybrid gamma 2a-gamma 2b heavy chains. It was found that both the polyclonal RF produced by autoimmune strains, MRL/MpJ-lpr and NZB/BinJ, and most of the monoclonal RF derived from normal strains, BALB/c, C57Bl/6, and 129/Sv, were directed against determinants located in a segment spanning the C-terminal 8 residues of the CH2 domain and the complete CH3 domain.
MeSH Terms
Animals
Antibodies, Monoclonal/immunology
Epitopes/immunology
Hybridomas/immunology
Immunoglobulin G/immunology
Immunoglobulin Heavy Chains/immunology
Immunoglobulin gamma-Chains/genetics,immunology
Mice
Mice, Inbred Strains
Mutation
Rheumatoid Factor/immunology
Chemicals
Antibodies, Monoclonal
Epitopes
Immunoglobulin G
Immunoglobulin Heavy Chains
Immunoglobulin gamma-Chains
Rheumatoid Factor
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Stassin V
Coulie P G
Birshtein B K
Secher D S
Van Snick J
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