ArticleProtein expression and purification2011
A Bacillus anthracis strain deleted for six proteases serves as an effective host for production of recombinant proteins.
Article in Protein expression and purification, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 52 citations in OpenAlex.
- Phase 1 study of a recombinant mutant protective antigen of Bacillus anthracis.Clinical and vaccine immunology : CVI · 2012Trial
- Caveolin 1 is a conserved host factor mediating Bacillus cereus hemolysin BL toxin cytolytic toxicity.PLoS biology · 2026Article
- Pathogenesis of human-derivedFrontiers in cellular and infection microbiology · 2026Article
- ERK pathway reactivation prevents anthrax toxin lethality in mice.Nature microbiology · 2025Article
- ATP depletion in anthrax edema toxin pathogenesis.PLoS pathogens · 2025Article
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- ERK and c-Myc signaling in host-derived tumor endothelial cells is essential for solid tumor growth.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Selective targeting of metastatic ovarian cancer using an engineered anthrax prodrug activated by membrane-anchored serine proteases.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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- Anthrax toxins regulate pain signaling and can deliver molecular cargoes into ANTXR2Nature neuroscience · 2022Article
- Identification of the transcription factor Miz1 as an essential regulator of diphthamide biosynthesis using a CRISPR-mediated genome-wide screen.PLoS genetics · 2020Article
- Integrated Transcriptomic and Proteomic Analyses Reveal the Role of NprR inFrontiers in microbiology · 2020Article
- Exploring the Nature of Cationic Blocker Recognition by the Anthrax Toxin Channel.Biophysical journal · 2019Article
- Distinct Contribution of the HtrA Protease and PDZ Domains to Its Function in Stress Resilience and Virulence ofFrontiers in microbiology · 2019Article
- InhA1-Mediated Cleavage of the Metalloprotease NprA AllowsFrontiers in microbiology · 2018Article
- Anti-tumor activity of anthrax toxin variants that form a functional translocation pore by intermolecular complementation.Oncotarget · 2017Article
- Article
- Anthrax Toxin Protective Antigen Variants That Selectively Utilize either the CMG2 or TEM8 Receptors for Cellular Uptake and Tumor Targeting.The Journal of biological chemistry · 2016Article
- Solid tumor therapy by selectively targeting stromal endothelial cells.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome.Structure (London, England : 1993) · 2016Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Bacillus anthracis produces a number of extracellular proteases that impact the integrity and yield of other proteins in the B. anthracis secretome. In this study we show that anthrolysin O (ALO) and the three anthrax toxin proteins, protective antigen (PA), lethal factor (LF), and edema factor (EF), produced from the B. anthracis Ames 35 strain (pXO1⁺, pXO2⁻), are completely degraded at the onset of stationary phase due to the action of proteases. An improved Cre-loxP gene knockout system was used to sequentially delete the genes encoding six proteases (InhA1, InhA2, camelysin, TasA, NprB, and MmpZ). The role of each protease in degradation of the B. anthracis toxin components and ALO was demonstrated. Levels of the anthrax toxin components and ALO in the supernatant of the sporulation defective, pXO1⁺ A35HMS mutant strain deleted for the six proteases were significantly increased and remained stable over 24 h. A pXO1-free variant of this six-protease mutant strain, designated BH460, provides an improved host strain for the preparation of recombinant proteins. As an example, BH460 was used to produce recombinant EF, which previously has been difficult to obtain from B. anthracis. The EF protein produced from BH460 had the highest in vivo potency of any EF previously purified from B. anthracis or Escherichia coli hosts. BH460 is recommended as an effective host strain for recombinant protein production, typically yielding greater than 10mg pure protein per liter of culture.
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