ArticleNature communications2015
The assembly dynamics of the cytolytic pore toxin ClyA.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 96 citations in OpenAlex.
- Cryo-EM structure of detergent-boundbioRxiv : the preprint server for biology · 2026Article
- Caveolin 1 is a conserved host factor mediating Bacillus cereus hemolysin BL toxin cytolytic toxicity.PLoS biology · 2026Article
- Inhalable engineered probiotic outer membrane vesicles co-expressing multiple mpox antigens induce potent specific systemic and mucosal immune responses.Materials today. Bio · 2026Article
- Circumventing the Impossible: Cell-Free Synthesis of Protein Toxins for Medical and Diagnostic Applications.International journal of molecular sciences · 2024Review
- Pore-Forming Proteins: From Pore Assembly to Structure by Quantitative Single-Molecule Imaging.International journal of molecular sciences · 2023Review
- Single-molecule tracking of perfringolysin O assembly and membrane insertion uncoupling.The FEBS journal · 2023Article
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- A look at the face of the molten globule: Structural model of the Helicobacter pylori apoflavodoxin ensemble at acidic pH.Protein science : a publication of the Protein Society · 2022Article
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- Polymerized porin as a novel delivery platform for coronavirus vaccine.Journal of nanobiotechnology · 2022Article
- Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Genomic Island of Vibrio cholerae Encodes a Three-Component Cytotoxin with Monomer and Protomer Forms Structurally Similar to Alpha-Pore-Forming Toxins.Journal of bacteriology · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- Labeling of Proteins for Single-Molecule Fluorescence Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021Review
- A tripartite cytolytic toxin formed byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- The Crystal Structure ofToxins · 2021Article
- Characterisation of a tripartite α-pore forming toxin from Serratia marcescens.Scientific reports · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pore-forming toxins are protein assemblies used by many organisms to disrupt the membranes of target cells. They are expressed as soluble monomers that assemble spontaneously into multimeric pores. However, owing to their complexity, the assembly processes have not been resolved in detail for any pore-forming toxin. To determine the assembly mechanism for the ring-shaped, homododecameric pore of the bacterial cytolytic toxin ClyA, we collected a diverse set of kinetic data using single-molecule spectroscopy and complementary techniques on timescales from milliseconds to hours, and from picomolar to micromolar ClyA concentrations. The entire range of experimental results can be explained quantitatively by a surprisingly simple mechanism. First, addition of the detergent n-dodecyl-β-D-maltopyranoside to the soluble monomers triggers the formation of assembly-competent toxin subunits, accompanied by the transient formation of a molten-globule-like intermediate. Then, all sterically compatible oligomers contribute to assembly, which greatly enhances the efficiency of pore formation compared with simple monomer addition.
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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.