ArticleBiochemistry2013
Monitoring the kinetics of the pH-driven transition of the anthrax toxin prepore to the pore by biolayer interferometry and surface plasmon resonance.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 26 citations in OpenAlex.
- Step-by-step maturation mechanism of the binary toxin pore revealed by cryo-EM analysis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Automated affinity selection for rapid discovery of peptide binders.Chemical science · 2021Article
- Anthrax toxin component, Protective Antigen, protects insects from bacterial infections.PLoS pathogens · 2020Article
- Article
- Role of a Small Molecule in the Modulation of Cell Death Signal Transduction Pathways.ACS infectious diseases · 2018Article
- Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy.Journal of visualized experiments : JoVE · 2018Article
- The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms.Frontiers in molecular biosciences · 2018Article
- Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain.Toxins · 2017Article
- Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins.Biochemistry · 2016Article
- Biochip for the Detection of Bacillus anthracis Lethal Factor and Therapeutic Agents against Anthrax Toxins.Membranes · 2016Article
- Roles of Anthrax Toxin Receptor 2 in Anthrax Toxin Membrane Insertion and Pore Formation.Toxins · 2016Review
- Molecular assembly of lethal factor enzyme and pre-pore heptameric protective antigen in early stage of translocation.Journal of molecular modeling · 2016Article
- Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs.The Journal of membrane biology · 2015Article
- Article
- Evaluation of Epic® label-free technology to quantify functional recombinant hemagglutinin.Biological procedures online · 2015Article
- Probing structurally altered and aggregated states of therapeutically relevant proteins using GroEL coupled to bio-layer interferometry.Protein science : a publication of the Protein Society · 2014Article
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
Abstract
Domain 2 of the anthrax protective antigen (PA) prepore heptamer unfolds and refolds during endosome acidification to generate an extended 100 Å β barrel pore that inserts into the endosomal membrane. The PA pore facilitates the pH-dependent unfolding and translocation of bound toxin enzymic components, lethal factor (LF) and/or edema factor, from the endosome to the cytoplasm. We constructed immobilized complexes of the prepore with the PA-binding domain of LF (LFN) to monitor the real-time prepore to pore kinetic transition using surface plasmon resonance and biolayer interferometry (BLI). The kinetics of this transition increased as the solution pH was decreased from 7.5 to 5.0, mirroring acidification of the endosome. Once it had undergone the transition, the LFN-PA pore complex was removed from the BLI biosensor tip and deposited onto electron microscopy grids, where PA pore formation was confirmed by negative stain electron microscopy. When the soluble receptor domain (ANTRX2/CMG2) binds the immobilized PA prepore, the transition to the pore state was observed only after the pH was lowered to early (pH 5.5) or late (pH 5.0) endosomal pH conditions. Once the pore formed, the soluble receptor readily dissociated from the PA pore. Separate binding experiments with immobilized PA pores and the soluble receptor indicate that the receptor has a weakened propensity to bind to the transitioned pore. This immobilized anthrax toxin platform can be used to identify or validate potential antimicrobial lead compounds capable of regulating and/or inhibiting anthrax toxin complex formation or pore transitions.
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