Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB

Bastian Bräuning (), Eva Bertosin, Florian Praetorius, Christian Ihling, Alexandra Schatt, Agnes Adler, Klaus Richter, Andrea Sinz, Hendrik Dietz and Michael Groll
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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

Nature Communications, 2018, vol. 9, issue 1, 1-14

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-04139-2

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