ArticleProtein engineering, design & selection : PEDS2012
High-level secretion of recombinant monomeric murine and human single-chain Fv antibodies from Drosophila S2 cells.
Article in Protein engineering, design & selection : PEDS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
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- Broadly neutralizing antibodies isolated from HEV convalescents confer protective effects in human liver-chimeric mice.Nature communications · 2025Article
- A human monoclonal antibody neutralizing SARS-CoV-2 Omicron variants containing the L452R mutation.Journal of virology · 2024Article
- Epitope-focused immunogens targeting the hepatitis C virus glycoproteins induce broadly neutralizing antibodies.Science advances · 2024Article
- Exclusion of Superinfection or Enhancement of Superinfection in Pestiviruses-APPV Infection Is Not Dependent on ADAM17.Viruses · 2024Article
- Article
- Structure, dynamics and transferability of the metal-dependent polyhistidine tetramerization motif TetrHis for single-chain Fv antibodies.Communications chemistry · 2023Article
- Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex.Science advances · 2022Article
- DNAJC14-Independent Replication of the Atypical Porcine Pestivirus.Journal of virology · 2022Article
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- Viral Traits and Cellular Knock-Out Genotype Affect Dependence of BVDV on Bovine CD46.Pathogens (Basel, Switzerland) · 2021Article
- Structural and Biophysical Characterization of the HCV E1E2 Heterodimer for Vaccine Development.Viruses · 2021Review
- Is LRP2 Involved in Leptin Transport over the Blood-Brain Barrier and Development of Obesity?International journal of molecular sciences · 2021Article
- Clinical and Serological Evaluation of LINDA Virus Infections in Post-Weaning Piglets.Viruses · 2019Article
- Species-Specific Functional Regions of the Green Alga Gamete Fusion Protein HAP2 Revealed by Structural Studies.Structure (London, England : 1993) · 2019Article
- Modifications of a signal sequence for antibody secretion from insect cells.Cytotechnology · 2018Article
- Computational Modeling of Hepatitis C Virus Envelope Glycoprotein Structure and Recognition.Frontiers in immunology · 2018Review
- Untargeted screening for novel autoantibodies with prognostic value in first-episode psychosis.Translational psychiatry · 2017Article
- Novel Pestivirus Species in Pigs, Austria, 2015.Emerging infectious diseases · 2017Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-chain variable fragment (scFvs) antibodies are small polypeptides (∼26 kD) containing the heavy (V(H)) and light (V(L)) immunoglobulin domains of a parent antibody connected by a flexible linker. In addition to being frequently used in diagnostics and therapy for an increasing number of human diseases, scFvs are important tools for structural biology as crystallization chaperones. Although scFvs can be expressed in many different organisms, the expression level of an scFv strongly depends on its particular amino acid sequence. We report here a system allowing for easy and efficient cloning of (i) scFvs selected by phage display and (ii) individual heavy and light chain sequences from hybridoma cDNA into expression plasmids engineered for secretion of the recombinant fragment produced in Drosophila S2 cells. We validated the method by producing five scFvs derived from human and murine parent antibodies directed against various antigens. The production yields varied between 5 and 12 mg monomeric scFv per liter of supernatant, indicating a relative independence on the individual sequences. The recombinant scFvs bound their cognate antigen with high affinity, comparable with the parent antibodies. The suitability of the produced recombinant fragments for structural studies was demonstrated by crystallization and structure determination of one of the produced scFvs, derived from a broadly neutralizing antibody against the major glycoprotein E2 of the hepatitis C virus. Structural comparison with the Protein Data Bank revealed the typical spatial organization of V(H) and V(L) domains, further validating the here-reported expression system.
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