Helical structure of the toxin MakA from Vibrio cholera
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ABSTRACT:
SUBMITTER: Jonas Barandun
PROVIDER: EMPIAR-10869 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Protein-lipid interaction at low pH induces oligomerization of the MakA cytotoxin from <i>Vibrio cholerae</i>.
Nadeem Aftab A Berg Alexandra A Pace Hudson H Alam Athar A Toh Eric E Ådén Jörgen J Zlatkov Nikola N Myint Si Lhyam SL Persson Karina K Gröbner Gerhard G Sjöstedt Anders A Bally Marta M Barandun Jonas J Uhlin Bernt Eric BE Wai Sun Nyunt SN
eLife 20220208
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 <i>Vibrio cholerae</i>. 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 grow ...[more]
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