ArticlePLoS pathogens2017
Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 70 citations in OpenAlex.
- Type VI Secretion Systems inMicroorganisms · 2026Article
- A heterotrimeric protein complex assembles the metazoan V-ATPase upon dissipation of proton gradients.Nature structural & molecular biology · 2025Article
- DMXL1 promotes recruitment of V1-ATPase to lysosomes upon TRPML1 activation.Nature structural & molecular biology · 2025Article
- Eeukaryotic-like Sppsk1 from Vibrio splendidus AJ01 mediates phagosome escape via inhibiting phagosome acidification and maturation.Cellular and molecular life sciences : CMLS · 2025Article
- ATG8ylation of vacuolar membrane protects plants against cell wall damage.Nature plants · 2025Article
- An acidic microenvironment produced by the V-type ATPase of Euprymna scolopes promotes specificity during Vibrio fischeri recruitment.Communications biology · 2024Article
- Structure of yeast RAVE bound to a partial VProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Advancements in Green Nanoparticle Technology: Focusing on the Treatment of Clinical Phytopathogens.Biomolecules · 2024Review
- Cigarette Smoking as a Risk Factor for Tuberculosis in Adults: Epidemiology and Aspects of Disease Pathogenesis.Pathogens (Basel, Switzerland) · 2024Review
- A model for collagen secretion by intercompartmental continuities.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The SARS-CoV-2 Spike Protein Mutation Explorer: using an interactive application to improve the public understanding of SARS-CoV-2 variants of concern.Journal of visual communication in medicine · 2023Article
- Replicative Acinetobacter baumannii strains interfere with phagosomal maturation by modulating the vacuolar pH.PLoS pathogens · 2023Article
- Eat or Be Eaten: Strategies Used byInfection and immunity · 2023Review
- ReplicativebioRxiv : the preprint server for biology · 2023Article
- Host-directed therapy for bacterial infections -Modulation of the phagolysosome pathway.Frontiers in immunology · 2023Review
- CryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7.Life science alliance · 2022Article
- Molecular design of a pathogen activated, self-assembling mechanopharmaceutical device.Journal of controlled release : official journal of the Controlled Release Society · 2022Review
- New Global Insights on the Regulation of the Biphasic Life Cycle and Virulence Via ClpP-Dependent Proteolysis in Legionella pneumophila.Molecular & cellular proteomics : MCP · 2022Article
- Coordinated conformational changes in the VNature structural & molecular biology · 2022Article
- Article
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular pathogenic bacteria evade the immune response by replicating within host cells. Legionella pneumophila, the causative agent of Legionnaires' Disease, makes use of numerous effector proteins to construct a niche supportive of its replication within phagocytic cells. The L. pneumophila effector SidK was identified in a screen for proteins that reduce the activity of the proton pumping vacuolar-type ATPases (V-ATPases) when expressed in the yeast Saccharomyces cerevisae. SidK is secreted by L. pneumophila in the early stages of infection and by binding to and inhibiting the V-ATPase, SidK reduces phagosomal acidification and promotes survival of the bacterium inside macrophages. We determined crystal structures of the N-terminal region of SidK at 2.3 Å resolution and used single particle electron cryomicroscopy (cryo-EM) to determine structures of V-ATPase:SidK complexes at ~6.8 Å resolution. SidK is a flexible and elongated protein composed of an α-helical region that interacts with subunit A of the V-ATPase and a second region of unknown function that is flexibly-tethered to the first. SidK binds V-ATPase strongly by interacting via two α-helical bundles at its N terminus with subunit A. In vitro activity assays show that SidK does not inhibit the V-ATPase completely, but reduces its activity by ~40%, consistent with the partial V-ATPase deficiency phenotype its expression causes in yeast. The cryo-EM analysis shows that SidK reduces the flexibility of the A-subunit that is in the 'open' conformation. Fluorescence experiments indicate that SidK binding decreases the affinity of V-ATPase for a fluorescent analogue of ATP. Together, these results reveal the structural basis for the fine-tuning of V-ATPase activity by SidK.
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