ArticleApplied and environmental microbiology2009
Direct expression of antimicrobial peptides in an intact form by a translationally coupled two-cistron expression system.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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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
7 citing papers in PubMed, 24 citations in OpenAlex.
- Secretory Production of Heterologous Antimicrobial Peptides inEngineering in life sciences · 2025Article
- Article
- Enhanced production of recombinant proteins in Corynebacterium glutamicum by constructing a bicistronic gene expression system.Microbial cell factories · 2020Article
- mRNA Engineering for the Efficient Chaperone-Mediated Co-Translational Folding of Recombinant Proteins inInternational journal of molecular sciences · 2019Article
- Cost-effective downstream processing of recombinantly produced pexiganan peptide and its antimicrobial activity.AMB Express · 2018Article
- Bicistronic expression strategy for high-level expression of recombinant proteins inEngineering in life sciences · 2017Article
- Overexpression of an antimicrobial peptide derived from C. elegans using an aggregation-prone protein coexpression system.AMB Express · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We describe a novel prokaryotic expression system for the production of cationic antimicrobial peptides (AMPs). The method relies on a translationally coupled two-cistron system, in which the termination codon for the first cistron (which encodes the anionic polypeptide mIFc2, a derivative of human gamma interferon) overlaps with the initiation codon for the second cistron (which encodes a cationic AMP) in the sequence of 5'-TAATG-3'. By forming an insoluble complex with the AMP upon translation, the mIFc2 protein efficiently neutralized the toxicity of the coexpressed cationic AMP and minimized the sensitivity of AMP to proteolytic degradation in a host. The AMPs were retrieved from the insoluble inclusion bodies without any chemical or enzymatic cleavage step by simple cation-exchange chromatography. With our system, approximately 100 mg of various AMPs (buforin IIb, parasin I, and pexiganan) were obtained from 1 liter of Escherichia coli culture. Our expression system may represent a universal cost-effective solution for the mass production of intact AMPs in their natural forms.
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Registered trials
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