ArticlePloS one2019
High-resolution cryo-EM structures of the E. coli hemolysin ClyA oligomers.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.
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Who cites it
20 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.
- Systematic review on the role of the gut microbiota in tumors and their treatment.Frontiers in endocrinology · 2024Pooled it
- Cryo-EM structure of detergent-boundbioRxiv : the preprint server for biology · 2026Article
- Tracking flaviviral protease conformational dynamics by tuning single-molecule nanopore tweezers.Biophysical journal · 2025Article
- A bacterial binary toxin system that kills both insects and aquatic crustaceans: Photorhabdus insect-related toxins A and B.PLoS pathogens · 2023Review
- Pore-Forming Proteins: From Pore Assembly to Structure by Quantitative Single-Molecule Imaging.International journal of molecular sciences · 2023Review
- Insights into the GSDMB-mediated cellular lysis and its targeting by IpaH7.8.Nature communications · 2023Article
- Atomic Force Microscopy Study of the Temperature and Storage Duration Dependencies of Horseradish Peroxidase Oligomeric State.Biomedicines · 2022Article
- Cryo-EM structure of a type IV secretion system.Nature · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021Review
- Article
- Review
- The Food Poisoning Toxins ofToxins · 2021Review
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
- Pore Forming Protein Induced Biomembrane Reorganization and Dynamics: A Focused Review.Frontiers in molecular biosciences · 2021Review
- The importance of the membrane for biophysical measurements.Nature chemical biology · 2020Review
- Article
- A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM.Nature structural & molecular biology · 2020Article
- Different Anomeric Sugar Bound States of Maltose Binding Protein Resolved by a Cytolysin A Nanopore Tweezer.ACS nano · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Pore-forming proteins (PFPs) represent a functionally important protein family, that are found in organisms from viruses to humans. As a major branch of PFPs, bacteria pore-forming toxins (PFTs) permeabilize membranes and usually cause the death of target cells. E. coli hemolysin ClyA is the first member with the pore complex structure solved among α-PFTs, employing α-helices as transmembrane elements. ClyA is proposed to form pores composed of various numbers of protomers. With high-resolution cryo-EM structures, we observe that ClyA pore complexes can exist as newly confirmed oligomers of a tridecamer and a tetradecamer, at estimated resolutions of 3.2 Å and 4.3 Å, respectively. The 2.8 Å cryo-EM structure of a dodecamer dramatically improves the existing structural model. Structural analysis indicates that protomers from distinct oligomers resemble each other and neighboring protomers adopt a conserved interaction mode. We also show a stabilized intermediate state of ClyA during the transition process from soluble monomers to pore complexes. Unexpectedly, even without the formation of mature pore complexes, ClyA can permeabilize membranes and allow leakage of particles less than ~400 Daltons. In addition, we are the first to show that ClyA forms pore complexes in the presence of cholesterol within artificial liposomes. These findings provide new mechanistic insights into the dynamic process of pore assembly for the prototypical α-PFT ClyA.
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Registered trials
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