ArticlemBio2012
Selective purification of recombinant neuroactive peptides using the flagellar type III secretion system.
Article in mBio, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
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
30 citing papers in PubMed.
- A bacteria-releasing mucoadhesive sheet for localized delivery and penetrative therapy of gastrointestinal cancer.Materials today. Bio · 2026Article
- Tumour-specific delivery of ω-conotoxin MVIIA via engineered Salmonella for safe anticancer therapy.Journal of advanced research · 2026Article
- AttenuatedActa pharmaceutica Sinica. B · 2026Article
- Laboratory Evolution Reveals Transcriptional Mechanisms Underlying Thermal Adaptation of Escherichia coli.Genome biology and evolution · 2025Article
- Engineering Bacterial Secretion Systems for Enhanced Tumor Imaging and Surgical Guidance.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Controlling tumor progression and recurrence in mice through combined treatment with a PD-L1 inhibitor and a designerActa pharmaceutica Sinica. B · 2024Article
- Bacterial-Based Cancer Therapy (BBCT): Recent Advances, Current Challenges, and Future Prospects for Cancer Immunotherapy.Vaccines · 2021Review
- Protein Export via the Type III Secretion System of the Bacterial Flagellum.Biomolecules · 2021Review
- Targeted Delivery of the Mitochondrial Target Domain of Noxa to Tumor Tissue via Synthetic Secretion System inFrontiers in bioengineering and biotechnology · 2020Article
- Engineering the flagellar type III secretion system: improving capacity for secretion of recombinant protein.Microbial cell factories · 2019Article
- Periplasmic Expression of 4/7 α-Conotoxin TxIA Analogs inFrontiers in pharmacology · 2019Article
- Developing Gram-negative bacteria for the secretion of heterologous proteins.Microbial cell factories · 2018Review
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
- An estimate is worth about a thousand experiments: using order-of-magnitude estimates to identify cellular engineering targets.Microbial cell factories · 2018Review
- Live attenuated Salmonella typhimurium vaccines delivering SaEsxA and SaEsxB via type III secretion system confer protection against Staphylococcus aureus infection.BMC infectious diseases · 2018Article
- Control of type III protein secretion using a minimal genetic system.Nature communications · 2017Article
- Proteins adopt functionally active conformations after type III secretion.Microbial cell factories · 2016Article
- Recombinant Expression and Characterization of α-Conotoxin LvIA in Escherichia coli.Marine drugs · 2016Article
- Bacteria in Cancer Therapy: Renaissance of an Old Concept.International journal of microbiology · 2016Review
- Type III secretion systems: the bacterial flagellum and the injectisome.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2015Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
unlabelledThe structure, assembly, and function of the bacterial flagellum involves about 60 different proteins, many of which are selectively secreted via a specific type III secretion system (T3SS) (J. Frye et al., J. Bacteriol. 188:2233-2243, 2006). The T3SS is reported to secrete proteins at rates of up to 10,000 amino acid residues per second. In this work, we showed that the flagellar T3SS of Salmonella enterica serovar Typhimurium could be manipulated to export recombinant nonflagellar proteins through the flagellum and into the surrounding medium. We translationally fused various neuroactive peptides and proteins from snails, spiders, snakes, sea anemone, and bacteria to the flagellar secretion substrate FlgM. We found that all tested peptides of various sizes were secreted via the bacterial flagellar T3SS. We subsequently purified the recombinant μ-conotoxin SIIIA (rSIIIA) from Conus striatus by affinity chromatography and confirmed that T3SS-derived rSIIIA inhibited mammalian voltage-gated sodium channel Na(V)1.2 comparably to chemically synthesized SIIIA. IMPORTANCE: Manipulation of the flagellar secretion system bypasses the problems of inclusion body formation and cellular degradation that occur during conventional recombinant protein expression. This work serves as a proof of principle for the use of engineered bacterial cells for rapid purification of recombinant neuroactive peptides and proteins by exploiting secretion via the well-characterized flagellator type III secretion system.
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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.