Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry
Web of Science
AuthorFabre, L; Santelli, E; Mountassif, D; Donoghue, A; Biswas, A; Blunck, R; Hanein, D; Volkmann, N; Liddington, R; Rouiller, I
Source TitleJournal of General Physiology
PublisherROCKEFELLER UNIV PRESS
University of Melbourne Author/sRouiller, Isabelle
AffiliationBiochemistry and Molecular Biology
Document TypeJournal Article
CitationsFabre, L., Santelli, E., Mountassif, D., Donoghue, A., Biswas, A., Blunck, R., Hanein, D., Volkmann, N., Liddington, R. & Rouiller, I. (2016). Structure of anthrax lethal toxin prepore complex suggests a pathway for efficient cell entry. JOURNAL OF GENERAL PHYSIOLOGY, 148 (4), pp.313-324. https://doi.org/10.1085/jgp.201611617.
Access StatusOpen Access
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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