Author
Listed:
- Bastian Bräuning
(Technische Universität München)
- Eva Bertosin
(Technische Universität München)
- Florian Praetorius
(Technische Universität München)
- Christian Ihling
(Martin-Luther University Halle-Wittenberg)
- Alexandra Schatt
(Martin-Luther University Halle-Wittenberg)
- Agnes Adler
(Technische Universität München)
- Klaus Richter
(Technische Universität München)
- Andrea Sinz
(Martin-Luther University Halle-Wittenberg)
- Hendrik Dietz
(Technische Universität München)
- Michael Groll
(Technische Universität München)
Abstract
Pore-forming toxins (PFT) are virulence factors that transform from soluble to membrane-bound states. The Yersinia YaxAB system represents a family of binary α-PFTs with orthologues in human, insect, and plant pathogens, with unknown structures. YaxAB was shown to be cytotoxic and likely involved in pathogenesis, though the molecular basis for its two-component lytic mechanism remains elusive. Here, we present crystal structures of YaxA and YaxB, together with a cryo-electron microscopy map of the YaxAB complex. Our structures reveal a pore predominantly composed of decamers of YaxA–YaxB heterodimers. Both subunits bear membrane-active moieties, but only YaxA is capable of binding to membranes by itself. YaxB can subsequently be recruited to membrane-associated YaxA and induced to present its lytic transmembrane helices. Pore formation can progress by further oligomerization of YaxA–YaxB dimers. Our results allow for a comparison between pore assemblies belonging to the wider ClyA-like family of α-PFTs, highlighting diverse pore architectures.
Suggested Citation
Bastian Bräuning & Eva Bertosin & Florian Praetorius & Christian Ihling & Alexandra Schatt & Agnes Adler & Klaus Richter & Andrea Sinz & Hendrik Dietz & Michael Groll, 2018.
"Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB,"
Nature Communications, Nature, vol. 9(1), pages 1-14, December.
Handle:
RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04139-2
DOI: 10.1038/s41467-018-04139-2
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