ArticleMolecular biotechnology2021
Autoinduction as Means for Optimization of the Heterologous Expression of Recombinant Single-Chain Fv (scFv) Antibodies.
Article in Molecular biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- C1q Is Recognized as a Soluble Autoantigen by Anti-C1q Antibodies of Patients with Systemic Lupus Erythematosus.Antibodies (Basel, Switzerland) · 2025Article
- Anti-C1q Autoantibody-Binding Engineered scFv C1q-Mimicking Fragment Enhances Disease Progression in Lupus-Prone MRL/lpr Mice.International journal of molecular sciences · 2025Article
- Article
- Development of alkaline phosphatase-linked single-chain variable fragment fusion proteins for one-step immunodetection of deoxynivalenol in cereals.Analytical and bioanalytical chemistry · 2024Article
- Application of an Autoinduction Strategy to Optimize the Heterologous Production of an Antitumor Bispecific Fusion Protein Based on the TRAIL Receptor-Selective Mutant Variant in Escherichia coli.Molecular biotechnology · 2023Article
- Anti-Idiotype scFv Localizes an Autoepitope in the Globular Domain of C1q.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The monoclonal antibodies and the recombinant antibody fragments are widely used in the biotechnology studies and in medicine as a powerful therapeutic and diagnostic tool. The most commonly used recombinant antibody fragments are single-chain fragment variable (scFv) because of their small size and minimal immunogenicity while still retaining high-affinity antigen binding. A wide range of expression systems such as bacterial and eukaryotic cell systems enable the sufficient production of scFv antibodies. However, their stable expression in soluble form and correct protein folding are often insufficient. In the present study, we present the autoinduction as a key element of the optimized scheme for heterologous expression of human monoclonal scFv antibodies (clones A1 and A12) in Escherichia coli HB2151, which resulted in two-fold increase of the total protein yield in 24 h.
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Registered trials
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