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TitleProtein-lipid interaction at low pH induces oligomerization of the MakA cytotoxin from .
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateFeb 8, 2022
AuthorsAftab Nadeem / Alexandra Berg / Hudson Pace / Athar Alam / Eric Toh / Jörgen Ådén / Nikola Zlatkov / Si Lhyam Myint / Karina Persson / Gerhard Gröbner / Anders Sjöstedt / Marta Bally / Jonas Barandun / Bernt Eric Uhlin / Sun Nyunt Wai /
PubMed AbstractThe α-pore-forming toxins (α-PFTs) from pathogenic bacteria damage host cell membranes by pore formation. We demonstrate a remarkable, hitherto unknown mechanism by an α-PFT protein from . As part ...The α-pore-forming toxins (α-PFTs) from pathogenic bacteria damage host cell membranes by pore formation. We demonstrate a remarkable, hitherto unknown mechanism by an α-PFT protein from . As part of the MakA/B/E tripartite toxin, MakA is involved in membrane pore formation similar to other α-PFTs. In contrast, MakA in isolation induces tube-like structures in acidic endosomal compartments of epithelial cells in vitro. The present study unravels the dynamics of tubular growth, which occurs in a pH-, lipid-, and concentration-dependent manner. Within acidified organelle lumens or when incubated with cells in acidic media, MakA forms oligomers and remodels membranes into high-curvature tubes leading to loss of membrane integrity. A 3.7 Å cryo-electron microscopy structure of MakA filaments reveals a unique protein-lipid superstructure. MakA forms a pinecone-like spiral with a central cavity and a thin annular lipid bilayer embedded between the MakA transmembrane helices in its active α-PFT conformation. Our study provides insights into a novel tubulation mechanism of an α-PFT protein and a new mode of action by a secreted bacterial toxin.
External linksElife / PubMed:35131030 / PubMed Central
MethodsEM (helical sym.)
Resolution3.65 Å
Structure data

13185

7p3r

EMDB-13185, PDB-7p3r:
Helical structure of the toxin MakA from Vibrio cholera
Method: EM (helical sym.) / Resolution: 3.65 Å

Source
  • vibrio cholerae o1 biovar el tor str. n16961 (bacteria)
  • Vibrio cholerae O1 biovar El Tor str. N16961
KeywordsTOXIN / Pore-forming toxin / Vibrio cholerae

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