ArticleThe Journal of general physiology2016
Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry.
Article in The Journal of general physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Solution Structures ofToxins · 2021Article
- Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors.Structure (London, England : 1993) · 2020Article
- Cryo-EM structure of the fully-loaded asymmetric anthrax lethal toxin in its heptameric pre-pore state.PLoS pathogens · 2020Article
- Impact of Bacterial Toxins in the Lungs.Toxins · 2020Review
- Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain.Toxins · 2017Article
- Anthrax lethal toxin co-complexes are stabilized by contacts between adjacent lethal factors.The Journal of general physiology · 2016Article
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10 authors.
Funding
Abstract
Anthrax toxin comprises three soluble proteins: protective antigen (PA), lethal factor (LF), and edema factor (EF). PA must be cleaved by host proteases before it oligomerizes and forms a prepore, to which LF and EF bind. After endocytosis of this tripartite complex, the prepore transforms into a narrow transmembrane pore that delivers unfolded LF and EF into the host cytosol. Here, we find that translocation of multiple 90-kD LF molecules is rapid and efficient. To probe the molecular basis of this translocation, we calculated a three-dimensional map of the fully loaded (PA63)7-(LF)3 prepore complex by cryo-electron microscopy (cryo-EM). The map shows three LFs bound in a similar way to one another, via their N-terminal domains, to the surface of the PA heptamer. The model also reveals contacts between the N- and C-terminal domains of adjacent LF molecules. We propose that this molecular arrangement plays an important role in the maintenance of translocation efficiency through the narrow PA pore.
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