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We demonstrate a remarkable, hitherto unknown mechanism by an \u03b1-PFT protein from\n                    <jats:italic>Vibrio cholerae<\/jats:italic>\n                    . As part of the MakA\/B\/E tripartite toxin, MakA is involved in membrane pore formation similar to other \u03b1-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 \u00c5 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 \u03b1-PFT conformation. Our study provides insights into a novel tubulation mechanism of an \u03b1-PFT protein and a new mode of action by a secreted bacterial toxin.\n                  <\/jats:p>","DOI":"10.7554\/elife.73439","type":"journal-article","created":{"date-parts":[[2022,1,20]],"date-time":"2022-01-20T10:15:14Z","timestamp":1642673714000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.73439","source":"Crossref","is-referenced-by-count":17,"title":["Protein-lipid interaction at low pH induces oligomerization of the MakA cytotoxin from Vibrio cholerae"],"prefix":"10.7554","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1439-6216","authenticated-orcid":true,"given":"Aftab","family":"Nadeem","sequence":"first","affiliation":[{"name":"Department of Molecular Biology, Ume\u00e5 University","place":["Ume\u00e5, Sweden"]},{"name":"Ume\u00e5 Centre for Microbial Research (UCMR), Ume\u00e5 University","place":["Ume\u00e5, Sweden"]},{"name":"The Laboratory for Molecular Infection Medicine 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