ArticleMicrobial cell factories2017
High-throughput expression of animal venom toxins in Escherichia coli to generate a large library of oxidized disulphide-reticulated peptides for drug discovery.
Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
- Engineered HMGB1 construct with tandem Box B domains promotes tissue regeneration without potential for inflammation.iScience · 2026Article
- Substrate Recognition Governs Reverse Transcriptase Resistance to Diagnostic Inhibitors in RT-qPCR.Diagnostics (Basel, Switzerland) · 2026Article
- From marine predator to pharmacology: Conotoxin diversity, discovery, and therapeutic potential.Zoological research · 2026Review
- Article
- Prospects and challenges of recombinant spider venom enzymes: insights fromFrontiers in bioengineering and biotechnology · 2025Article
- ADDovenom: Thermostable Protein-Based ADDomer Nanoparticles as New Therapeutics for Snakebite Envenoming.Toxins · 2023Article
- Article
- Holistic profiling of the venom from the Brazilian wandering spiderFrontiers in molecular biosciences · 2023Article
- A ShK-like Domain fromToxins · 2022Article
- Modern venomics-Current insights, novel methods, and future perspectives in biological and applied animal venom research.GigaScience · 2022Article
- Generation of a Library of Carbohydrate-Active Enzymes for Plant Biomass Deconstruction.International journal of molecular sciences · 2022Article
- Stability and Safety of Inhibitor Cystine Knot Peptide, GTx1-15, from the Tarantula SpiderToxins · 2021Article
- Development of a Broad-Spectrum Antiserum against Cobra Venoms Using Recombinant Three-Finger Toxins.Toxins · 2021Article
- Strategies for the Production of Soluble Interferon-AlphaLife (Basel, Switzerland) · 2021Article
- Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins.Frontiers in bioengineering and biotechnology · 2021Review
- Animal toxins - Nature's evolutionary-refined toolkit for basic research and drug discovery.Biochemical pharmacology · 2020Review
- Curses or Cures: A Review of the Numerous Benefits Versus the Biosecurity Concerns of Conotoxin Research.Biomedicines · 2020Review
- Expression of Melittin in Fusion with GST inACS omega · 2020Article
- Expression, Purification and Docking Studies on IMe-AGAP, the First Antitumor-analgesic Like Peptide from Iranian ScorpionIranian journal of pharmaceutical research : IJPR · 2020Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAnimal venoms are complex molecular cocktails containing a wide range of biologically active disulphide-reticulated peptides that target, with high selectivity and efficacy, a variety of membrane receptors. Disulphide-reticulated peptides have evolved to display improved specificity, low immunogenicity and to show much higher resistance to degradation than linear peptides. These properties make venom peptides attractive candidates for drug development. However, recombinant expression of reticulated peptides containing disulphide bonds is challenging, especially when associated with the production of large libraries of bioactive molecules for drug screening. To date, as an alternative to artificial synthetic chemical libraries, no comprehensive recombinant libraries of natural venom peptides are accessible for high-throughput screening to identify novel therapeutics.
resultsIn the accompanying paper an efficient system for the expression and purification of oxidized disulphide-reticulated venom peptides in Escherichia coli is described. Here we report the development of a high-throughput automated platform, that could be adapted to the production of other families, to generate the largest ever library of recombinant venom peptides. The peptides were produced in the periplasm of E. coli using redox-active DsbC as a fusion tag, thus allowing the efficient formation of correctly folded disulphide bridges. TEV protease was used to remove fusion tags and recover the animal venom peptides in the native state. Globally, within nine months, out of a total of 4992 synthetic genes encoding a representative diversity of venom peptides, a library containing 2736 recombinant disulphide-reticulated peptides was generated. The data revealed that the animal venom peptides produced in the bacterial host were natively folded and, thus, are putatively biologically active.
conclusionsOverall this study reveals that high-throughput expression of animal venom peptides in E. coli can generate large libraries of recombinant disulphide-reticulated peptides of remarkable interest for drug discovery programs.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.