ArticleMicrobiologyOpen2016
Identification of regions within the Legionella pneumophila VipA effector protein involved in actin binding and polymerization and in interference with eukaryotic organelle trafficking.
Article in MicrobiologyOpen, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- The small GTPase Rab5 inhibits actin polymerization mediated by the Legionella pneumophila effector VipA.Medical microbiology and immunology · 2026Article
- Screening bacterial effectors and human virus proteins in yeast to identify host factors driving tombusvirus RNA recombination: a role for autophagy and membrane phospholipid content.Journal of virology · 2025Article
- Review
- A comprehensive two-hybrid analysis to explore themSystems · 2024Article
- Membrane-dependent actin polymerization mediated by thebioRxiv : the preprint server for biology · 2023Article
- Functional Mimicry of Eukaryotic Actin Assembly by Pathogen Effector Proteins.International journal of molecular sciences · 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
- Article
- Ectopic Expression of Human Thymosin β4 Confers Resistance to Legionella pneumophila during Pulmonary and Systemic Infection in Mice.Infection and immunity · 2021Article
- Article
- Extracellular Actin Is a Receptor forFrontiers in cellular and infection microbiology · 2018Article
- Identification of regions within the Legionella pneumophila VipA effector protein involved in actin binding and polymerization and in interference with eukaryotic organelle trafficking.MicrobiologyOpen · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Legionella pneumophila effector protein VipA is an actin nucleator that co-localizes with actin filaments and early endosomes in infected macrophages and which interferes with organelle trafficking when expressed in yeast. To identify the regions of VipA involved in its subcellular localization and functions, we ectopically expressed specific VipA mutant proteins in eukaryotic cells. This indicated that the characteristic punctate distribution of VipA depends on its NH2 -terminal (amino acid residues 1-133) and central coiled-coil (amino acid residues 133-206) regions, and suggested a role for the COOH-terminal (amino acid residues 206-339) region in association with actin filaments and for the NH2 -terminal in co-localization with early endosomes. Co-immunoprecipitation and in vitro assays showed that the COOH-terminal region of VipA is necessary and sufficient to mediate actin binding, and is essential but insufficient to induce microfilament formation. Assays in yeast revealed that the NH2 and the COOH-terminal regions, and possibly an NPY motif within the NH2 region of VipA, are necessary for interference with organelle trafficking. Overall, this suggests that subversion of eukaryotic vesicular trafficking by VipA involves both its ability to associate with early endosomes via its NH2 -terminal region and its capacity to bind and polymerize actin through its COOH-terminal region.
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