ArticleProtein science : a publication of the Protein Society2009
Engineering antibody fragments to fold in the absence of disulfide bonds.
Article in Protein science : a publication of the Protein Society, 2009. 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, 30 citations in OpenAlex.
- 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
- Luminescence Fingerprint of Intracellular NIR-II Gold Nanocluster Transformation: Implications for Sensing and Imaging.ACS nano · 2025Article
- A Shiga Toxin B-Subunit-Based Lectibody Boosts T Cell Cytotoxicity towards Gb3-Positive Cancer Cells.Cells · 2023Article
- Disulfide-compatible phage-assisted continuous evolution in the periplasmic space.Nature communications · 2021Article
- Continuous directed evolution of proteins with improved soluble expression.Nature chemical biology · 2018Article
- Exploration of broadly neutralizing antibody fragments produced in bacteria for the control of HIV.Human vaccines & immunotherapeutics · 2017Article
- Construction of polyomavirus-derived pseudotype virus-like particles displaying a functionally active neutralizing antibody against hepatitis B virus surface antigen.BMC biotechnology · 2015Article
- Strain engineering for improved expression of recombinant proteins in bacteria.Microbial cell factories · 2011Review
- Exploiting cross-reactivity to neutralize two different scorpion venoms with one single chain antibody fragment.The Journal of biological chemistry · 2011Article
- Protein aggregation profile of the bacterial cytosol.PloS one · 2010Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide bonds play a critical role in the stabilization of the immunoglobulin beta-sandwich sandwich. Under reducing conditions, such as those that prevail in the cytoplasm, disulfide bonds do not normally form and as a result most antibodies expressed in that compartment (intrabodies) accumulate in a misfolded and inactive state. We have developed a simple method for the quantitative isolation of antibody fragments that retain full activity under reducing conditions from large mutant libraries. In E. coli, inactivation of the cysteine oxidoreductase DsbA abolishes protein oxidation in the periplasm, which leads to the accumulation of scFvs and other disulfide-containing proteins in a reduced form. Libraries of mutant scFvs were tethered onto the inner membrane of dsbA cells and mutants that could bind fluorescently labeled antigen in the reducing periplasm were screened by Anchored Periplasmic Expression (APEx; Harvey et al., Proc Natl Acad Sci USA 2004;101:9193-9198.). Using this approach, we isolated scFv antibody variants that are fully active when expressed in the cytoplasm or when the four Cys residues that normally form disulfides are substituted by Ser residues.
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