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• W2024702860 endingPage "210" @default.
• W2024702860 startingPage "197" @default.
• W2024702860 abstract "Antibodies H241 and 2C10 are lupus mouse IgG autoantibodies that bind native DNA. In previous experiments, oligonucleotide antigens affinity-labeled both H and L chains of H241 but only the H chain of antibody 2C10. Primary structures of the V regions of the 2C10 H and L chains and the H241 L chain, determined from cDNA, help to explain the previous affinity-labeling experiments. The 2C10 L chain CDRs had several Asp residues and a net negative charge of five, whereas the 2C10 H chain CDRs had four Arg residues and a net positive charge of five. The L chain CDRs of H241 had a net positive charge of one. [The H241 H chain cDNA sequence was published previously by Gangemi et al. (1993) J. Immun. 151, 4660-4671]. Plasmid vectors were used for bacterial expression of H and L chains of 2C10 alone and in combinations in single chain Fv (scFv) molecules. The H chain alone bound native DNA as well as or better than the H-plus-L chain scFv. The H chain alone also bound Z-DNA. Combination of the 2C10 H chain with the L chain of an anti-Z-DNA antibody maintained the selectivity for Z-DNA, whereas its combination with the 2C10 L chain (in the 2C10 Fab) yielded selective B-DNA binding. The results with 2C10 match other examples in which the H chain is sufficient for DNA binding but selectivity is modulated by the L chain. The H chain binding to autoantigen may reflect selective events in early stages of B cell development." @default.
• W2024702860 created "2016-06-24" @default.
• W2024702860 creator A5008942832 @default.
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• W2024702860 date "1996-02-01" @default.
• W2024702860 modified "2023-09-27" @default.
• W2024702860 title "Heavy chain dominance in the binding of DNA by a lupus mouse monoclonal autoantibody" @default.
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• W2024702860 doi "https://doi.org/10.1016/0161-5890(95)00094-1" @default.
• W2024702860 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8649441" @default.
• W2024702860 hasPublicationYear "1996" @default.
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