6h2e › Citations

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)
Related entries: 6grj, 6grk, 6h2d, 6h2f, 6r1j

Cited: 13 times
EuropePMC logo PMID: 31263098

Abstract

The alpha helical CytolysinA family of pore forming toxins (α-PFT) contains single, two, and three component members. Structures of the single component Eschericia coli ClyA and the two component Yersinia enterolytica YaxAB show both undergo conformational changes from soluble to pore forms, and oligomerization to produce the active pore. Here we identify tripartite α-PFTs in pathogenic Gram negative bacteria, including Aeromonas hydrophila (AhlABC). We show that the AhlABC toxin requires all three components for maximal cell lysis. We present structures of pore components which describe a bi-fold hinge mechanism for soluble to pore transition in AhlB and a contrasting tetrameric assembly employed by soluble AhlC to hide their hydrophobic membrane associated residues. We propose a model of pore assembly where the AhlC tetramer dissociates, binds a single membrane leaflet, recruits AhlB promoting soluble to pore transition, prior to AhlA binding to form the active hydrophilic lined pore.

Articles - 6h2e mentioned but not cited (3)

  1. 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)
  2. A tripartite cytolytic toxin formed by Vibrio cholerae proteins with flagellum-facilitated secretion. Nadeem A, Nagampalli R, Toh E, Alam A, Myint SL, Heidler TV, Dongre M, Zlatkov N, Pace H, Bano F, Sjöstedt A, Bally M, Uhlin BE, Wai SN, Persson K. Proc Natl Acad Sci U S A 118 e2111418118 (2021)
  3. 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)


Reviews citing this publication (3)

  1. The Food Poisoning Toxins of Bacillus cereus. Dietrich R, Jessberger N, Ehling-Schulz M, Märtlbauer E, Granum PE. Toxins (Basel) 13 98 (2021)
  2. 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)
  3. Cytolysin A (ClyA): A Bacterial Virulence Factor with Potential Applications in Nanopore Technology, Vaccine Development, and Tumor Therapy. Murase K. Toxins (Basel) 14 78 (2022)

Articles citing this publication (7)

  1. Bacterial pore-forming toxins. Ulhuq FR, Mariano G. Microbiology (Reading) 168 (2022)
  2. 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)
  3. The A component (SmhA) of a tripartite pore-forming toxin from Serratia marcescens: expression, purification and crystallographic analysis. Churchill-Angus AM, Sedelnikova SE, Schofield THB, Baker PJ. Acta Crystallogr F Struct Biol Commun 76 577-582 (2020)
  4. Crystal structure and activity of a de novo enzyme, ferric enterobactin esterase Syn-F4. Kurihara K, Umezawa K, Donnelly AE, Sperling B, Liao G, Hecht MH, Arai R. Proc Natl Acad Sci U S A 120 e2218281120 (2023)
  5. Presence and function of Hbl B', the fourth protein component encoded by the hbl operon in Bacillus cereus. Jessberger N, Diedrich R, Janowski R, Niessing D, Märtlbauer E. Virulence 13 483-501 (2022)
  6. 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)
  7. V. cholerae MakA is a cholesterol-binding pore-forming toxin that induces non-canonical autophagy. Jia X, Knyazeva A, Zhang Y, Castro-Gonzalez S, Nakamura S, Carlson LA, Yoshimori T, Corkery DP, Wu YW. J Cell Biol 221 e202206040 (2022)


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