ArticleNature microbiology2024
Stepwise assembly and release of Tc toxins from Yersinia entomophaga.
Article in Nature microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- Article
- Non-lytic protein secretion by virulence-associated Type 10 Secretion Systems inFrontiers in microbiology · 2026Article
- Visualizing Postsynaptic Density in Excitatory Synapses with Electron Tomography.Advances in neurobiology · 2026Review
- A targeted cell lysis mechanism facilitates toxin release in Clostridioides difficile.bioRxiv : the preprint server for biology · 2025Article
- Article
- Cryo-electron tomography: en route to the molecular anatomy of organisms and tissues.Biochemical Society transactions · 2024Review
- Review
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Tc toxins are virulence factors of bacterial pathogens. Although their structure and intoxication mechanism are well understood, it remains elusive where this large macromolecular complex is assembled and how it is released. Here we show by an integrative multiscale imaging approach that Yersinia entomophaga Tc (YenTc) toxin components are expressed only in a subpopulation of cells that are 'primed' with several other potential virulence factors, including filaments of the protease M66/StcE. A phage-like lysis cassette is required for YenTc release; however, before resulting in complete cell lysis, the lysis cassette generates intermediate 'ghost' cells, which may serve as assembly compartments and become packed with assembled YenTc holotoxins. We hypothesize that this stepwise mechanism evolved to minimize the number of cells that need to be killed. The occurrence of similar lysis cassettes in diverse organisms indicates a conserved mechanism for Tc toxin release that may apply to other extracellular macromolecular machines.
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Registered trials
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