Preferential association of κIIIb light chains with monoclonal human IgMκ autoantibodies

D. K. Ledford, F. Goni, M. Pizzolato, E. C. Franklin, Alan Solomon, B. Frangione

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Abstract

The predominance of the relatively uncommon V region subgroup isotype κIII among the light chains of human monoclonal (IgMκ) anti-IgG antibodies, (i.e., rheumatoid factors), was further documented through sequence analyses of ten such autoantibodies isolated from IgM-anti-IgG cold-insoluble immune complexes (mixed cryoglobulins). The amino-terminal sequence of all ten κ-chains was characteristic for κIII proteins and virtually identical to that of a prototype κIII light chain. Similar sequence identity was found for κ-chains isolated from three IgMκ autoantibodies that formed cold-insoluble immune complexes with low-density lipoprotein (LDL). The thirteen light chains were found to be virtually identical in sequence for the first framework region (FR); ten of these proteins sequenced through the first complementarity-determining region (CDR) and into the second FR were markedly similar. The second CDR of five proteins was almost identical in sequence to that of the phototype κIII-chain. Concordance was also demonstrated between the structural classification of the light chains as κIII members of this V region subgroup. Serologic analyses of light chains isolated from seven IgMκ autoantibodies (six anti-IgG, one anti-LDL) and of one intact IgMκ anti-LDL antibody showed that each had antigenic determinants common to κIII proteins. These light chains also expressed the antigenic determinant(s) of a V-region sub-subgroup of κIII proteins designated κIIIb. Our studies confirm the preferential association of κIII (and κIIIb) light chains with IgMκ anti-IgG antibodies and demonstrate a similar association for IgMκ anti-LDL antibodies. The finding that these and other types of IgMκ autoantibodies, e.g., cold agglutinins, have remarkably similar light chains suggests an inherent restriction in the immune response to self-antigens.

Original languageEnglish (US)
Pages (from-to)1322-1325
Number of pages4
JournalJournal of Immunology
Volume131
Issue number3
StatePublished - Oct 13 1983

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Autoantibodies
Immunoglobulin M
Light
LDL Lipoproteins
Complementarity Determining Regions
Antigen-Antibody Complex
Proteins
Epitopes
Anti-Idiotypic Antibodies
Cryoglobulins
Antibodies
Rheumatoid Factor
Autoantigens
Sequence Analysis
anti-IgG

All Science Journal Classification (ASJC) codes

  • Immunology

Cite this

Ledford, D. K., Goni, F., Pizzolato, M., Franklin, E. C., Solomon, A., & Frangione, B. (1983). Preferential association of κIIIb light chains with monoclonal human IgMκ autoantibodies. Journal of Immunology, 131(3), 1322-1325.

Preferential association of κIIIb light chains with monoclonal human IgMκ autoantibodies. / Ledford, D. K.; Goni, F.; Pizzolato, M.; Franklin, E. C.; Solomon, Alan; Frangione, B.

In: Journal of Immunology, Vol. 131, No. 3, 13.10.1983, p. 1322-1325.

Research output: Contribution to journalArticle

Ledford, DK, Goni, F, Pizzolato, M, Franklin, EC, Solomon, A & Frangione, B 1983, 'Preferential association of κIIIb light chains with monoclonal human IgMκ autoantibodies', Journal of Immunology, vol. 131, no. 3, pp. 1322-1325.
Ledford DK, Goni F, Pizzolato M, Franklin EC, Solomon A, Frangione B. Preferential association of κIIIb light chains with monoclonal human IgMκ autoantibodies. Journal of Immunology. 1983 Oct 13;131(3):1322-1325.
Ledford, D. K. ; Goni, F. ; Pizzolato, M. ; Franklin, E. C. ; Solomon, Alan ; Frangione, B. / Preferential association of κIIIb light chains with monoclonal human IgMκ autoantibodies. In: Journal of Immunology. 1983 ; Vol. 131, No. 3. pp. 1322-1325.
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abstract = "The predominance of the relatively uncommon V region subgroup isotype κIII among the light chains of human monoclonal (IgMκ) anti-IgG antibodies, (i.e., rheumatoid factors), was further documented through sequence analyses of ten such autoantibodies isolated from IgM-anti-IgG cold-insoluble immune complexes (mixed cryoglobulins). The amino-terminal sequence of all ten κ-chains was characteristic for κIII proteins and virtually identical to that of a prototype κIII light chain. Similar sequence identity was found for κ-chains isolated from three IgMκ autoantibodies that formed cold-insoluble immune complexes with low-density lipoprotein (LDL). The thirteen light chains were found to be virtually identical in sequence for the first framework region (FR); ten of these proteins sequenced through the first complementarity-determining region (CDR) and into the second FR were markedly similar. The second CDR of five proteins was almost identical in sequence to that of the phototype κIII-chain. Concordance was also demonstrated between the structural classification of the light chains as κIII members of this V region subgroup. Serologic analyses of light chains isolated from seven IgMκ autoantibodies (six anti-IgG, one anti-LDL) and of one intact IgMκ anti-LDL antibody showed that each had antigenic determinants common to κIII proteins. These light chains also expressed the antigenic determinant(s) of a V-region sub-subgroup of κIII proteins designated κIIIb. Our studies confirm the preferential association of κIII (and κIIIb) light chains with IgMκ anti-IgG antibodies and demonstrate a similar association for IgMκ anti-LDL antibodies. The finding that these and other types of IgMκ autoantibodies, e.g., cold agglutinins, have remarkably similar light chains suggests an inherent restriction in the immune response to self-antigens.",
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AU - Goni, F.

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AU - Solomon, Alan

AU - Frangione, B.

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AB - The predominance of the relatively uncommon V region subgroup isotype κIII among the light chains of human monoclonal (IgMκ) anti-IgG antibodies, (i.e., rheumatoid factors), was further documented through sequence analyses of ten such autoantibodies isolated from IgM-anti-IgG cold-insoluble immune complexes (mixed cryoglobulins). The amino-terminal sequence of all ten κ-chains was characteristic for κIII proteins and virtually identical to that of a prototype κIII light chain. Similar sequence identity was found for κ-chains isolated from three IgMκ autoantibodies that formed cold-insoluble immune complexes with low-density lipoprotein (LDL). The thirteen light chains were found to be virtually identical in sequence for the first framework region (FR); ten of these proteins sequenced through the first complementarity-determining region (CDR) and into the second FR were markedly similar. The second CDR of five proteins was almost identical in sequence to that of the phototype κIII-chain. Concordance was also demonstrated between the structural classification of the light chains as κIII members of this V region subgroup. Serologic analyses of light chains isolated from seven IgMκ autoantibodies (six anti-IgG, one anti-LDL) and of one intact IgMκ anti-LDL antibody showed that each had antigenic determinants common to κIII proteins. These light chains also expressed the antigenic determinant(s) of a V-region sub-subgroup of κIII proteins designated κIIIb. Our studies confirm the preferential association of κIII (and κIIIb) light chains with IgMκ anti-IgG antibodies and demonstrate a similar association for IgMκ anti-LDL antibodies. The finding that these and other types of IgMκ autoantibodies, e.g., cold agglutinins, have remarkably similar light chains suggests an inherent restriction in the immune response to self-antigens.

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