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The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane
Open accessPreprint — published as 10.1038/s41467-022-32992-9 · Paper page
Abstract
Enteric bacteria have to adapt to environmental stresses in the human gastrointestinal tract such as acid and nutrient stress, oxygen limitation and exposure to antibiotics. Membrane lipid composition has recently emerged as a key factor for stress adaptation. The E. coli ravA-viaA operon is essential for aminoglycoside bactericidal activity under anaerobiosis but its mechanism of action is unclear. Here we characterise the VWA domain-protein ViaA and its interaction with the AAA+ ATPase RavA, and find that both proteins localise at the inner cell membrane. We demonstrate that RavA and ViaA target specific phospholipids and subsequently identify their lipid-binding sites. We further show that mutations abolishing interaction with lipids restore induced changes in cell membrane morphology and lipid composition. Finally we reveal that these mutations render E. coli gentamicin-resistant under fumarate respiration conditions. Our work thus uncovers a ravA-viaA -based pathway which is mobilised in response to antibiotics under anaerobiosis and has a major impact on cell membrane regulation.
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Metadata
- Authors
- Felix, J., Bumba, L., Liesche, C., Fraudeau, A., Rébeillé, F., El Khoury, J. Y., Huard, K., Gallet, B., Moriscot, C., Kleman, J.-P., Duhoo, Y., Jessop, M., Kandiah, E., Barras, F., Jouhet, J., & Gutsche, I.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Gutsche, Irina
- ORCID
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2022-02-06
- Volume
- 13
- Issue
- 1
- Pages
- 5502-5502
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9489729
- OpenAlex
- W4296774165
- Cited by
- 7
- References
- 1
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 4
- FWCI
- 0.91
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Infrastructures en Biologie Santé et Agronomie (ANR-17-EURE-0003)
- European Commission (ANR-17-EURE-0003, LX22NPO5103, UAR 3518 CNRS-CEA-UGA-EMBL, 789385, 647784, HORIZON2020)
- Agence Nationale de la Recherche (ANR-10-INSB-05-01., UAR 3518 CNRS-CEA-UGA-EMBL, ANR-17-EURE-0003, 10-INSB-05-01, ANR- 10-INSB-05, ANR-17-EURE-, ANR-17, ANR-10, ANR-10-INBS-0005, ANR-10-LABX-0049)
- Ministerstvo Školství, Mládeže a Tělovýchovy (LM2018133)
- Centre National de la Recherche Scientifique (ANR‐17‐EURE‐0003, UAR 3518 CNRS-CEA-UGA-EMBL)
- French Infrastructure for Integrated Structural Biology (UAR 3518 CNRS-CEA-UGA-EMBL, ANR-17-EURE-0003, ANR-10-INBS-0005, ANR-10- INSB-05, ANR-10-INSB-0501, ANR-10-INBS-000502, INSB-05, ANR-10-INBS)
- Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement
- H2020 Marie Skłodowska-Curie Actions (ANR-17-EURE-0003, HORIZON2020)
- NextGenerationEU
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Health Sciences › Medicine › Microbiology (medical) › Antibiotic Resistance in Bacteria
- Keywords
- Rava, AAA+ ATPase, VWA domain, gentamicin resistance, Escherichia coli, inner membrane, membrane lipid composition, lipid binding sites, membrane morphology, anaerobic stress, fumarate respiration, stress adaptation
- MeSH terms
- ATPases Associated with Diverse Cellular Activities, Adenosine Triphosphatases, Aminoglycosides, Anti-Bacterial Agents, Escherichia coli, Fumarates, Gentamicins, Membrane Lipids, Oxygen, Phospholipids, Escherichia coli Proteins
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