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Protein-lipid interaction at low pH induces oligomerization of the MakA cytotoxin from Vibrio cholerae
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).ORCID iD: 0000-0002-1439-6216
Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS).ORCID iD: 0000-0003-3609-2878
Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Medicine, Department of Clinical Microbiology. Umeå University, Faculty of Medicine, Wallenberg Centre for Molecular Medicine at Umeå University (WCMM).ORCID iD: 0000-0001-5116-2577
Umeå University, Faculty of Medicine, Department of Clinical Microbiology. Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR).ORCID iD: 0000-0001-8773-7598
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2022 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 11, article id e73439Article in journal (Refereed) Published
Abstract [en]

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 Vibrio cholerae. 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.

Place, publisher, year, edition, pages
eLife Sciences Publications, Ltd , 2022. Vol. 11, article id e73439
Keywords [en]
Vibrio cholerae, MakA, lipid
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-192300DOI: 10.7554/eLife.73439Scopus ID: 2-s2.0-85124321786OAI: oai:DiVA.org:umu-192300DiVA, id: diva2:1635905
Funder
Swedish Research Council, 2018–02914Swedish Research Council, 2016–05009Swedish Research Council, 2019–01720Swedish Research Council, 2016–06963Swedish Research Council, 2019–02011Swedish Cancer Society, 2017–419Swedish Cancer Society, 2020–711The Kempe Foundations, JCK-1728The Kempe Foundations, SMK-1756.2The Kempe Foundations, SMK-1553The Kempe Foundations, JCK-1724The Kempe Foundations, SMK-1961Knut and Alice Wallenberg FoundationFamiljen Erling-Perssons StiftelseAvailable from: 2022-02-08 Created: 2022-02-08 Last updated: 2024-01-12Bibliographically approved

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Nadeem, AftabBerg, AlexandraPace, HudsonAlam, AtharToh, EricÅdén, JörgenZlatkov, NikolaMyint, Si LhyamPersson, KarinaGröbner, GerhardSjöstedt, AndersBally, MartaBarandun, JonasUhlin, Bernt EricWai, Sun Nyunt

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Nadeem, AftabBerg, AlexandraPace, HudsonAlam, AtharToh, EricÅdén, JörgenZlatkov, NikolaMyint, Si LhyamPersson, KarinaGröbner, GerhardSjöstedt, AndersBally, MartaBarandun, JonasUhlin, Bernt EricWai, Sun Nyunt
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Department of Molecular Biology (Faculty of Medicine)Umeå Centre for Microbial Research (UCMR)Molecular Infection Medicine Sweden (MIMS)Department of Clinical MicrobiologyWallenberg Centre for Molecular Medicine at Umeå University (WCMM)Department of ChemistryClinical Bacteriology
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