Dataset Information
Helical structure of the toxin MakA from Vibrio cholera
Ontology highlight
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>.
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]