ReviewFrontiers in microbiology2020
Solubility, Stability, and Avidity of Recombinant Antibody Fragments Expressed in Microorganisms.
Review in Frontiers in microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 82 citations in OpenAlex.
- Multidimensional maturation of antibody variable domains with machine-learning assistance.mAbs · 2026Article
- Human monoclonal and polyclonal anti-ADAMTS13 antibodies in immune thrombotic thrombocytopenic purpura: variable mechanisms of inhibition.Journal of thrombosis and haemostasis : JTH · 2026Article
- Improvement in binding and function of a monoclonal antibody against Shigella flexneri 3a O-antigen via phage display and whole-cell in-solution panning.The Journal of biological chemistry · 2026Article
- Extracellular vesicle-based delivery to airway basal cells for durable gene therapy in cystic fibrosis.Frontiers in bioengineering and biotechnology · 2026Review
- Evaluation of recombinant extracellular enveloped virion protein candidates for the detection of serological responses to lumpy skin disease virus in cattle.The veterinary quarterly · 2025Article
- A Bidirectional EF1 Promoter System for Armoring CD19 CAR-T Cells with Secreted Anti-PD1 Antibodies.International journal of molecular sciences · 2025Article
- High-throughput synthesis and specificity characterization of natively paired influenza hemagglutinin antibodies with oPoolScience translational medicine · 2025Article
- Designing a multi-epitope vaccine against African swine fever virus using immunoinformatics approach.Scientific reports · 2025Article
- Integrating Biochemical and Computational Approaches Reveal Structural Insights in Trastuzumab scFv-Fc Antibody Engineering.Biomolecules · 2025Article
- Revolutionizing oncology: the role of Artificial Intelligence (AI) as an antibody design, and optimization tools.Biomarker research · 2025Review
- Unveiling the new chapter in nanobody engineering: advances in traditional construction and AI-driven optimization.Journal of nanobiotechnology · 2025Review
- In silico designing and optimization of anti-epidermal growth factor receptor scaffolds by complementary-determining regions-grafting technique.Quantitative biology (Beijing, China) · 2024Article
- Controlled labelling of tracer antibodies for time-resolved fluorescence-based immunoassays.Scientific reports · 2024Article
- Fit-for-purpose heterodivalent single-domain antibody for gastrointestinal targeting of toxin B from Clostridium difficile.Protein science : a publication of the Protein Society · 2024Article
- Development, High-Throughput Profiling, and Biopanning of a Large Phage Display Single-Domain Antibody Library.International journal of molecular sciences · 2024Article
- Review
- Monoclonal Antibodies as a Therapeutic Strategy against Multidrug-Resistant Bacterial Infections in a Post-COVID-19 Era.Life (Basel, Switzerland) · 2024Review
- Generation of a Recombinant scFv against Deoxycholic Acid and Its Conversion to a Quenchbody for One-Step Immunoassay.Methods and protocols · 2023Article
- Phage display technology for fabricating a recombinant monoclonal ScFv antibody against tetanus toxin.Toxicology research · 2023Article
- Optimization and Characterization of Novel ALCAM-Targeting Antibody Fragments for Transepithelial Delivery.Pharmaceutics · 2023Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Solubility of recombinant proteins (i.e., the extent of soluble versus insoluble expression in heterogeneous hosts) is the first checkpoint criterion for determining recombinant protein quality. However, even soluble proteins often fail to represent functional activity because of the involvement of non-functional, misfolded, soluble aggregates, which compromise recombinant protein quality. Therefore, screening of solubility and folding competence is crucial for improving the quality of recombinant proteins, especially for therapeutic applications. The issue is often highlighted especially in bacterial recombinant hosts, since bacterial cytoplasm does not provide an optimal environment for the folding of target proteins of mammalian origin. Antibody fragments, such as single-chain variable fragment (scFv), single-chain antibody (scAb), and fragment antigen binding (Fab), have been utilized for numerous applications such as diagnostics, research reagents, or therapeutics. Antibody fragments can be efficiently expressed in microorganisms so that they offer several advantages for diagnostic applications such as low cost and high yield. However, scFv and scAb fragments have generally lower stability to thermal stress than full-length antibodies, necessitating a judicious combination of designer antibodies, and bacterial hosts harnessed with robust chaperone function. In this review, we discuss efforts on not only the production of antibodies or antibody fragments in microorganisms but also scFv stabilization via (i) directed evolution of variants with increased stability using display systems, (ii) stabilization of the interface between variable regions of heavy (V
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.