ArticleNature chemical biology2013
Disulfide-bond scanning reveals assembly state and β-strand tilt angle of the PFO β-barrel.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Hexameric-Based Hierarchy in the Sizes of a Cytolysin Pore-Forming Complex.Biomolecules · 2025Article
- Visualizing the Domino-Like Prepore-to-Pore Transition of Streptolysin O by High-Speed AFM.The Journal of membrane biology · 2023Article
- Cholesterol-dependent cytolysins: The outstanding questions.IUBMB life · 2022Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- A Key Motif in the Cholesterol-Dependent Cytolysins Reveals a Large Family of Related Proteins.mBio · 2020Article
- Inerolysin and vaginolysin, the cytolysins implicated in vaginal dysbiosis, differently impair molecular integrity of phospholipid membranes.Scientific reports · 2019Article
- Article
- Cholesterol-dependent cytolysins: from water-soluble state to membrane pore.Biophysical reviews · 2018Review
- Conformational folding and disulfide bonding drive distinct stages of protein structure formation.Scientific reports · 2018Article
- CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin.eLife · 2017Article
- Domain 4 (D4) of Perfringolysin O to Visualize Cholesterol in Cellular Membranes-The Update.Sensors (Basel, Switzerland) · 2017Review
- Revealing Assembly of a Pore-Forming Complex Using Single-Cell Kinetic Analysis and Modeling.Biophysical journal · 2016Article
- Review
- Structure of the poly-C9 component of the complement membrane attack complex.Nature communications · 2016Article
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
- Stonefish toxin defines an ancient branch of the perforin-like superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Single molecule compression reveals intra-protein forces drive cytotoxin pore formation.eLife · 2015Article
- Decreasing Transmembrane Segment Length Greatly Decreases Perfringolysin O Pore Size.The Journal of membrane biology · 2015Article
- Review
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
Perfringolysin O (PFO), a bacterial cholesterol-dependent cytolysin, binds a mammalian cell membrane, oligomerizes into a circular prepore complex (PPC) and forms a 250-Å transmembrane β-barrel pore in the cell membrane. Each PFO monomer has two sets of three short α-helices that unfold and ultimately refold into two transmembrane β-hairpin (TMH) components of the membrane-embedded β-barrel. Interstrand disulfide-bond scanning revealed that β-strands in a fully assembled PFO β-barrel were strictly aligned and tilted at 20° to the membrane perpendicular. In contrast, in a low temperature-trapped PPC intermediate, the TMHs were unfolded and had sufficient freedom of motion to interact transiently with each other, yet the TMHs were not aligned or stably hydrogen bonded. The PFO PPC-to-pore transition therefore converts TMHs in a dynamic folding intermediate far above the membrane into TMHs that are hydrogen bonded to those of adjacent subunits in the bilayer-embedded β-barrel.
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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.