ArticleNature communications2022
A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 26 citations in OpenAlex.
- Structure-coevolution dual-guided engineering of C-glycosyltransferase enables high-level biosynthesis of vitexin inSynthetic and systems biotechnology · 2026Article
- Improving purity and apparent thermal stability of single-chain Fv antibodies by heat treatment in a soluble E. coli cytoplasmic expression system.Journal of biochemistry · 2026Article
- Two-in-one protein tag enables the soluble expression and calcium-dependent purification of single-chain antibody fragments.Communications biology · 2026Article
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- CHO-K1 cell-derived scFv targeting pseudorabies virus ameliorates multi-organ viremia and improves animal survival in a lethal infection model.Frontiers in microbiology · 2026Article
- Article
- Digital Microfluidics-Driven Cell-Free Protein Synthesis Platform Reveals Expression and Stability Determinants for Phytoglobins and Cysteine-to-Alanine Substituted Variants.Antioxidants (Basel, Switzerland) · 2025Article
- Screening microorganisms with robust and stable protein expression and secretion capacity.Protein science : a publication of the Protein Society · 2025Article
- miR-3188 inhibits hepatitis B virus transcription by targeting Bcl-2.Archives of virology · 2024Article
- Identification of an N-terminal tag (580N) that improves the biosynthesis of fluorescent proteins in Francisella tularensis and other Gram-negative bacteria.Molecular and cellular probes · 2024Article
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Authors and funding
16 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-chain variable fragments (scFvs), composed of variable domains of heavy and light chains of an antibody joined by a linker, share antigen binding capacity with their parental antibody. Due to intrinsically low solubility and stability, only two Escherichia coli-produced scFvs have been approved for therapy. Here we report that a 33-residue peptide, termed P17 tag, increases the solubility of multiple scFvs produced in Escherichia coli SHuffle strain by up to 11.6 fold. Hydrophilic sequence, especially charged residues, but not the predicted α-helical secondary structure of P17 tag, contribute to the solubility enhancement. Notably, the P17 tag elevates the thermostability of scFv as efficiently as intra-domain disulfide bonds. Moreover, a P17-tagged scFv targeting hepatitis B virus surface proteins shows over two-fold higher antigen-binding affinity and virus-neutralizing activity than the untagged version. These data strongly suggest a type I intramolecular chaperone-like activity of the P17 tag. Hence, the P17 tag could benefit the research, production, and application of scFv.
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