ArticleNature2015
Atomic structure of anthrax protective antigen pore elucidates toxin translocation.
Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.
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Who cites it
141 citing papers in PubMed, 261 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
- Beyond the Static Caliper: Dynamical Translocases and the Mathematical Imperative for Single-Molecule Proteomics.bioRxiv : the preprint server for biology · 2026Article
- Structural basis for independent pore function of Vpb4 from Bacillus thuringiensis.Nature communications · 2026Article
- Rational Engineering of the Anthrax Toxin Nanopore Interface for Orthogonal Peptide Classification.ACS omega · 2026Article
- Structural basis for the assembly and translocation of the Vip1-Vip2 insecticidal toxin from Bacillus thuringiensis.Nature communications · 2026Article
- Peptide properties predict multistate translocation kinetics via protective antigen nanopores.Biophysical journal · 2026Article
- Identification and structural characterization of anthrax toxin receptor 2 as the Clostridium perfringens NetF receptor.Nature communications · 2026Article
- Dynamic gating by ϕ-clamp loop controls peptide translocation through the anthrax toxin nanopore.Biophysical journal · 2026Article
- A dynamical anthrax toxin nanopore biosensor for high-fidelity single-peptide classification.PLoS computational biology · 2026Article
- Chimeric Antibody Engineering AgainstToxins · 2026Article
- Intraluminal Vesicles as Transfection Intermediaries.Pharmaceutics · 2025Article
- Single-molecule sensing with an anthrax nanopore enabled by pH-asymmetric ionic liquids.Journal of nanobiotechnology · 2025Article
- Anthrax Toxin: A Pioneer of Targeted Protein Toxins.Toxins · 2025Review
- Structural insights into pre-pore intermediates of alpha-hemolysin in the lipidic environment.Nature communications · 2025Article
- Particle dynamics in biconical cavities: First-passage, direct-transit, and looping time distributions.The Journal of chemical physics · 2025Article
- The Biological Role of Conoporins, Actinoporin-like Pore-Forming Toxins from Cone Snails.Toxins · 2025Review
- Antiviral siRNA delivered using attenuated, anthrax toxin protects cells from the cytopathic effects of Zika virus.Virus genes · 2025Article
- Accessibility of Carboxypeptidase A-bound Zinc to Chelation Correlates with an Intermediate State in the Protein's Unfolding Pathway.Biochemistry · 2025Article
- The N-terminus of themBio · 2025Article
- Deep learning-based classification of peptide analytes from single-channel nanopore translocation events.PloS one · 2025Article
81 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
Anthrax toxin, comprising protective antigen, lethal factor, and oedema factor, is the major virulence factor of Bacillus anthracis, an agent that causes high mortality in humans and animals. Protective antigen forms oligomeric prepores that undergo conversion to membrane-spanning pores by endosomal acidification, and these pores translocate the enzymes lethal factor and oedema factor into the cytosol of target cells. Protective antigen is not only a vaccine component and therapeutic target for anthrax infections but also an excellent model system for understanding the mechanism of protein translocation. On the basis of biochemical and electrophysiological results, researchers have proposed that a phi (Φ)-clamp composed of phenylalanine (Phe)427 residues of protective antigen catalyses protein translocation via a charge-state-dependent Brownian ratchet. Although atomic structures of protective antigen prepores are available, how protective antigen senses low pH, converts to active pore, and translocates lethal factor and oedema factor are not well defined without an atomic model of its pore. Here, by cryo-electron microscopy with direct electron counting, we determine the protective antigen pore structure at 2.9-Å resolution. The structure reveals the long-sought-after catalytic Φ-clamp and the membrane-spanning translocation channel, and supports the Brownian ratchet model for protein translocation. Comparisons of four structures reveal conformational changes in prepore to pore conversion that support a multi-step mechanism by which low pH is sensed and the membrane-spanning channel is formed.
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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.