ArticleProceedings of the National Academy of Sciences of the United States of America1997
The antigen-binding domain of a human IgG-anti-F(ab')2 autoantibody.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Natural autoimmunity in oligoarticular juvenile idiopathic arthritis.Pediatric rheumatology online journal · 2023Article
- Antibody Affinity and Stability Maturation by Error-Prone PCR.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Construction of Human Immune and Naive scFv Phage Display Libraries.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Molecular characterization of human anti-hinge antibodies derived from single-cell cloning of normal human B cells.The Journal of biological chemistry · 2018Article
- Modular Construction of Large Non-Immune Human Antibody Phage-Display Libraries from Variable Heavy and Light Chain Gene Cassettes.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Soluble T-cell receptor design influences functional yield in an E. coli chaperone-assisted expression system.PloS one · 2018Article
- Designing Human Antibodies by Phage Display.Transfusion medicine and hemotherapy : offizielles Organ der Deutschen Gesellschaft fur Transfusionsmedizin und Immunhamatologie · 2017Review
- Beyond citrullination: other post-translational protein modifications in rheumatoid arthritis.Nature reviews. Rheumatology · 2017Review
- Joining the in vitro immunization of alpaca lymphocytes and phage display: rapid and cost effective pipeline for sdAb synthesis.Microbial cell factories · 2017Article
- DeltaPhage--a novel helper phage for high-valence pIX phagemid display.Nucleic acids research · 2012Article
- Silicon photonic crystal nanocavity-coupled waveguides for error-corrected optical biosensing.Biosensors & bioelectronics · 2011Article
- Novel evolved immunoglobulin (Ig)-binding molecules enhance the detection of IgM against hepatitis C virus.PloS one · 2011Article
- Expanding the versatility of phage display I: efficient display of peptide-tags on protein VII of the filamentous phage.PloS one · 2011Article
- Article
- Rise and fall of an anti-MUC1 specific antibody.PloS one · 2011Article
- Antibody expressing pea seeds as fodder for prevention of gastrointestinal parasitic infections in chickens.BMC biotechnology · 2009Article
- Quantitative evaluation of sensitivity and selectivity of multiplex nanoSPR biosensor assays.Biophysical journal · 2007Article
- On the influence of vector design on antibody phage display.Journal of biotechnology · 2007Article
- Generation and production of engineered antibodies.Molecular biotechnology · 2004Review
- Recombinant antibodies for the diagnosis and treatment of cancer.Molecular biotechnology · 2003Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies revealed an immunoregulatory role of natural IgG-anti-F(ab')2 antibodies in both healthy individuals and patients with certain diseases. The implication of anti-F(ab')2 antibodies in the pathogenesis of diseases prompted us to study the gene segment structure of their antigen-binding domains and their binding characteristics. cDNA was prepared from the lymphocytes of a patient with a high IgG-anti-F(ab')2 serum titer. Variable heavy and light gene segments were amplified by PCR and inserted into a phagemid surface expression vector. Single-chain antibodies displayed on the phage surface were screened for binding to F(ab')2 fragments. The subsequent analysis of 95 single clones demonstrated that they all bound specifically to F(ab')2. Sequence analyses of 12 clones showed that 11 were identical and 1 contained a silent point mutation in the heavy chain and three amino acid exchanges in the light chain. The heavy chains belonged to the V(H)3 and the light chains to the V(kappa)2 gene family. The 11 identical light-chain genes were completely homologous to a germ-line sequence (DPK-15). Binding assays showed that the single-chain antibodies bind to F(ab')2, but not to Fab, Fc, or intact IgG. This binding pattern was confirmed by surface plasmon resonance studies, which revealed a relatively high affinity (Ka = 2.8 x 10(7) M(-1)). The strong binding capacity was further demonstrated by competitive inhibition of the serum anti-IgG antibody's interaction with antigen. The present study defines for the first time to our knowledge the gene segment structure of the antigen-binding domain of two human IgG-anti-F(ab')2 autoantibody clones and describes the binding kinetics of the purified monomeric fragments.
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