Framework peptides from kappa IIIb rheumatoid factor light chains with binding activity for aggregated IgG.
Most monoclonal human rheumatoid factors (RF) and some RF from rheumatoid patient's synovia are restricted in their light chains, using predominantly the kappa IIIb subfamily. Very few sequence differences are found between these light chains. Light chains with similar variable region framework sequences are also found in some mouse monoclonal RF derived from mice stimulated with lipopolysaccharide or secondarily immunized with protein antigens. There are two likely explanations for this restriction in framework sequences between the two species: (a) the sequences are important for the immunoregulation of RF production or (b) the sequences are concerned with the antibody binding specificity of the RF. We have examined overlapping octapeptides from the kappa IIIb light chain variable region and show that some framework peptides have the ability to bind aggregated IgG. Replacement of amino acids within the peak binding peptide have indicated the critical amino acids necessary for binding.
Hay
F C
FC
Division of Immunology, St George's Hospital Medical School, London, Great Britain.
Soltys
A J
AJ
Tribbick
G
G
Geysen
H M
HM
D000595:Amino Acid Sequence; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D007147:Immunoglobulin Light Chains / Q000378:metabolism*; D007145:Immunoglobulin kappa-Chains / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism*; D012217:Rheumatoid Factor / Q000378:metabolism*
D007074:Immunoglobulin G; D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains; D010446:Peptide Fragments; C044411:polymeric IgG; D012217:Rheumatoid Factor