ArticleMicrobial cell factories2017
Gene design, fusion technology and TEV cleavage conditions influence the purification of oxidized disulphide-rich venom peptides in Escherichia coli.
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 27 papers.
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Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
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- ADDovenom: Thermostable Protein-Based ADDomer Nanoparticles as New Therapeutics for Snakebite Envenoming.Toxins · 2023Article
- Expression, Purification and Characterization of Functional Teduglutide Using GST Fusion System in Prokaryotic Cells.Advanced pharmaceutical bulletin · 2023Article
- The structure of aJournal of structural biology: X · 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
- Recombinant expression of hen egg white lysozyme with the assistance of xylanase fusion partner inBioengineered · 2022Article
- Generation of a Library of Carbohydrate-Active Enzymes for Plant Biomass Deconstruction.International journal of molecular sciences · 2022Article
- Co-delivery of genes can be confounded by bicistronic vector design.MRS communications · 2022Article
- Stability and Safety of Inhibitor Cystine Knot Peptide, GTx1-15, from the Tarantula SpiderToxins · 2021Article
- Effective production of human growth factors in Escherichia coli by fusing with small protein 6HFh8.Microbial cell factories · 2021Article
- Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins.Frontiers in bioengineering and biotechnology · 2021Review
- Acoustic biosensors for ultrasound imaging of enzyme activity.Nature chemical biology · 2020Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAnimal venoms are large, complex libraries of bioactive, disulphide-rich peptides. These peptides, and their novel biological activities, are of increasing pharmacological and therapeutic importance. However, recombinant expression of venom peptides in Escherichia coli remains difficult due to the significant number of cysteine residues requiring effective post-translational processing. There is also an urgent need to develop high-throughput recombinant protocols applicable to the production of reticulated peptides to enable efficient screening of their drug potential. Here, a comprehensive study was developed to investigate how synthetic gene design, choice of fusion tag, compartment of expression, tag removal conditions and protease recognition site affect levels of solubility of oxidized venom peptides produced in E. coli.
resultsThe data revealed that expression of venom peptides imposes significant pressure on cysteine codon selection. DsbC was the best fusion tag for venom peptide expression, in particular when the fusion was directed to the bacterial periplasm. While the redox activity of DsbC was not essential to maximize expression of recombinant fusion proteins, redox activity did lead to higher levels of correctly folded target peptides. With the exception of proline, the canonical TEV protease recognition site tolerated all other residues at its C-terminus, confirming that no non-native residues, which might affect activity, need to be incorporated at the N-terminus of recombinant peptides for tag removal.
conclusionsThis study reveals that E. coli is a convenient heterologous host for the expression of soluble and functional venom peptides. Using the optimal construct design, a large and diverse range of animal venom peptides were produced in the µM scale. These results open up new possibilities for the high-throughput production of recombinant disulphide-rich peptides in E. coli.
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