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

Bräuning B, Bertosin E, Praetorius F, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M
Nat Commun 9 1806 (2018)
Related entries: 6ek4, 6ek8, 6el1

Cited: 29 times
EuropePMC logo PMID: 29728606

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.

Reviews - 6ek7 mentioned but not cited (2)

  1. Structural Basis of the Pore-Forming Toxin/Membrane Interaction. Li Y, Li Y, Mengist HM, Shi C, Zhang C, Wang B, Li T, Huang Y, Xu Y, Jin T. Toxins (Basel) 13 128 (2021)
  2. Structural and Mechanistic Features of ClyA-Like α-Pore-Forming Toxins. Bräuning B, Groll M. Toxins (Basel) 10 (2018)

Articles - 6ek7 mentioned but not cited (5)

  1. Structure and mechanism of the two-component α-helical pore-forming toxin YaxAB. Bräuning B, Bertosin E, Praetorius F, Ihling C, Schatt A, Adler A, Richter K, Sinz A, Dietz H, Groll M. Nat Commun 9 1806 (2018)
  2. Membrane insertion of α-xenorhabdolysin in near-atomic detail. Schubert E, Vetter IR, Prumbaum D, Penczek PA, Raunser S. Elife 7 (2018)
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  1. Beyond pore formation: reorganization of the plasma membrane induced by pore-forming proteins. Kulma M, Anderluh G. Cell Mol Life Sci 78 6229-6249 (2021)
  2. Pore-Forming Toxins During Bacterial Infection: Molecular Mechanisms and Potential Therapeutic Targets. Hu H, Liu M, Sun S. Drug Des Devel Ther 15 3773-3781 (2021)
  3. Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance. Gupta LK, Molla J, Prabhu AA. Mol Biotechnol (2023)
  4. Toxigenic Properties of Yersinia enterocolitica Biotype 1A. Platt-Samoraj A. Toxins (Basel) 14 118 (2022)

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  2. Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane. Byrne MJ, Iadanza MG, Perez MA, Maskell DP, George RM, Hesketh EL, Beales PA, Zack MD, Berry C, Thompson RF. Nat Commun 12 2791 (2021)
  3. The Crystal Structure of Bacillus cereus HblL1. Worthy HL, Williamson LJ, Auhim HS, Leppla SH, Sastalla I, Jones DD, Rizkallah PJ, Berry C. Toxins (Basel) 13 253 (2021)
  4. CASP13 target classification into tertiary structure prediction categories. Kinch LN, Kryshtafovych A, Monastyrskyy B, Grishin NV. Proteins 87 1021-1036 (2019)
  5. Characterisation of a tripartite α-pore forming toxin from Serratia marcescens. Churchill-Angus AM, Schofield THB, Marlow TR, Sedelnikova SE, Wilson JS, Rafferty JB, Baker PJ. Sci Rep 11 6447 (2021)
  6. A Genomic Island of Vibrio cholerae Encodes a Three-Component Cytotoxin with Monomer and Protomer Forms Structurally Similar to Alpha-Pore-Forming Toxins. Herrera A, Kim Y, Chen J, Jedrzejczak R, Shukla S, Maltseva N, Joachimiak G, Welk L, Wiersum G, Jaroszewski L, Godzik A, Joachimiak A, Satchell KJF. J Bacteriol 204 e0055521 (2022)
  7. Evolution of Structural Biology through the Lens of Mass Spectrometry. Kaur U, Johnson DT, Chea EE, Deredge DJ, Espino JA, Jones LM. Anal. Chem. 91 142-155 (2019)
  8. A coiled-coil-based design strategy for the thermostabilization of G-protein-coupled receptors. Amer M, Leka O, Jasko P, Frey D, Li X, Kammerer RA. Sci Rep 13 10159 (2023)
  9. Direct Quantification of Damaged Nucleotides in Oligonucleotides Using an Aerolysin Single Molecule Interface. Wang J, Li MY, Yang J, Wang YQ, Wu XY, Huang J, Ying YL, Long YT. ACS Cent Sci 6 76-82 (2020)
  10. FALCON2: a web server for high-quality prediction of protein tertiary structures. Kong L, Ju F, Zhang H, Sun S, Bu D. BMC Bioinformatics 22 439 (2021)
  11. High-resolution cryo-EM structures of the E. coli hemolysin ClyA oligomers. Peng W, de Souza Santos M, Li Y, Tomchick DR, Orth K. PLoS ONE 14 e0213423 (2019)
  12. Identification and structural analysis of the tripartite α-pore forming toxin of Aeromonas hydrophila. Wilson JS, Churchill-Angus AM, Davies SP, Sedelnikova SE, Tzokov SB, Rafferty JB, Bullough PA, Bisson C, Baker PJ. Nat Commun 10 2900 (2019)
  13. Pore-forming Esx proteins mediate toxin secretion by Mycobacterium tuberculosis. Tak U, Dokland T, Niederweis M. Nat Commun 12 394 (2021)
  14. Protein Sizing with 15 nm Conical Biological Nanopore YaxAB. Straathof S, Di Muccio G, Yelleswarapu M, Alzate Banguero M, Wloka C, van der Heide NJ, Chinappi M, Maglia G. ACS Nano 17 13685-13699 (2023)
  15. Protein-lipid interaction at low pH induces oligomerization of the MakA cytotoxin from Vibrio cholerae. Nadeem A, Berg A, Pace H, Alam A, Toh E, Ådén J, Zlatkov N, Myint SL, Persson K, Gröbner G, Sjöstedt A, Bally M, Barandun J, Uhlin BE, Wai SN. Elife 11 e73439 (2022)
  16. Single-molecule fingerprinting of protein-drug interaction using a funneled biological nanopore. Jeong KB, Ryu M, Kim JS, Kim M, Yoo J, Chung M, Oh S, Jo G, Lee SG, Kim HM, Lee MK, Chi SW. Nat Commun 14 1461 (2023)
  17. Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer. Sengupta N, Mondal AK, Mishra S, Chattopadhyay K, Dutta S. J Cell Biol 220 e202102035 (2021)
  18. Structure of the Lysinibacillus sphaericus Tpp49Aa1 pesticidal protein elucidated from natural crystals using MHz-SFX. Williamson LJ, Galchenkova M, Best HL, Bean RJ, Munke A, Awel S, Pena G, Knoska J, Schubert R, Dörner K, Park HW, Bideshi DK, Henkel A, Kremling V, Klopprogge B, Lloyd-Evans E, Young MT, Valerio J, Kloos M, Sikorski M, Mills G, Bielecki J, Kirkwood H, Kim C, de Wijn R, Lorenzen K, Xavier PL, Rahmani Mashhour A, Gelisio L, Yefanov O, Mancuso AP, Federici BA, Chapman HN, Crickmore N, Rizkallah PJ, Berry C, Oberthür D. Proc Natl Acad Sci U S A 120 e2203241120 (2023)


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