ArticleJournal of industrial microbiology & biotechnology2015
Expression and one-step purification of the antimicrobial peptide cathelicidin-BF using the intein system in Bacillus subtilis.
Article in Journal of industrial microbiology & biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Cathelicidins: Opportunities and Challenges in Skin Therapeutics and Clinical Translation.Antibiotics (Basel, Switzerland) · 2024Review
- High expression of antimicrobial peptides cathelicidin-BF inFrontiers in microbiology · 2023Article
- The future of recombinant host defense peptides.Microbial cell factories · 2022Review
- Antimicrobial Peptides from Plants: A cDNA-Library Based Isolation, Purification, Characterization Approach and Elucidating Their Modes of Action.International journal of molecular sciences · 2021Review
- Strategies for Optimizing the Production of Proteins and Peptides with Multiple Disulfide Bonds.Antibiotics (Basel, Switzerland) · 2020Review
- Review
- Cathelicidins: Immunomodulatory Antimicrobials.Vaccines · 2018Review
- Highly efficient soluble expression, purification and characterization of recombinant Aβ42 fromRSC advances · 2018Article
- Expression of plectasin in Bacillus subtilis using SUMO technology by a maltose-inducible vector.Journal of industrial microbiology & biotechnology · 2015Article
- A novel expression vector for the secretion of abaecin in Bacillus subtilis.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intein expression system has been widely applied in Escherichia coli to express various proteins and peptides. However, the removal of endotoxin from the recombinant proteins expressed in E. coli is very difficult and therefore complicates the purification process. In this study, we constructed an intein-based expression vector for an antimicrobial peptide (cathelicidin from Bungarus fasciatus) and expressed the intein fusion peptide in a Bacillus subtilis expression system. The fusion peptide was secreted into the culture medium, identified by Western blot and purified by affinity chromatography and intein self-cleavage in just one step. Approximately, 0.5 mg peptide was obtained from 1 litre of culture medium. The purified peptide showed antimicrobial activity. Our results indicate that the intein expression system may be a safe and efficient method to produce soluble peptides and proteins in B. subtilis.
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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.