ArticlePloS one2014
Polar localization of PhoN2, a periplasmic virulence-associated factor of Shigella flexneri, is required for proper IcsA exposition at the old bacterial pole.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 38 citations in OpenAlex.
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- Molecular mechanisms of Shigella effector proteins: a common pathogen among diarrheic pediatric population.Molecular and cellular pediatrics · 2022Review
- Selection for Phage Resistance Reduces Virulence of Shigella flexneri.Applied and environmental microbiology · 2022Article
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- Extracellular ATP as an Inter-Kingdom Signaling Molecule: Release Mechanisms by Bacteria and Its Implication on the Host.International journal of molecular sciences · 2020Review
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- Establishment of a Protein Concentration Gradient in the Outer Membrane Requires Two Diffusion-Limiting Mechanisms.Journal of bacteriology · 2019Article
- ATP released by intestinal bacteria limits the generation of protective IgA against enteropathogens.Nature communications · 2019Article
- A bet-hedging strategy for denitrifying bacteria curtails their release of NProceedings of the National Academy of Sciences of the United States of America · 2018Article
- T Follicular Helper Cells Promote a Beneficial Gut Ecosystem for Host Metabolic Homeostasis by Sensing Microbiota-Derived Extracellular ATP.Cell reports · 2017Article
- The Intriguing Evolutionary Journey of EnteroinvasiveFrontiers in microbiology · 2017Review
- TheBiochemistry and biophysics reports · 2016Article
- Molecular and Cellular Mechanisms of Shigella flexneri Dissemination.Frontiers in cellular and infection microbiology · 2016Review
- The Multifaceted Activity of the VirF Regulatory Protein in theFrontiers in molecular biosciences · 2016Review
- Analysis on the interaction domain of VirG and apyrase by pull-down assay.Molecules (Basel, Switzerland) · 2014Article
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11 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Proper protein localization is critical for bacterial virulence. PhoN2 is a virulence-associated ATP-diphosphohydrolase (apyrase) involved in IcsA-mediated actin-based motility of S. flexneri. Herein, by analyzing a ΔphoN2 mutant of the S. flexneri strain M90T and by generating phoN2::HA fusions, we show that PhoN2, is a periplasmic protein that strictly localizes at the bacterial poles, with a strong preference for the old pole, the pole where IcsA is exposed, and that it is required for proper IcsA exposition. PhoN2-HA was found to be polarly localized both when phoN2::HA was ectopically expressed in a Escherichia coli K-12 strain and in a S. flexneri virulence plasmid-cured mutant, indicating a conserved mechanism of PhoN2 polar delivery across species and that neither IcsA nor the expression of other virulence-plasmid encoded genes are involved in this process. To assess whether PhoN2 and IcsA may interact, two-hybrid and cross-linking experiments were performed. While no evidence was found of a PhoN2-IcsA interaction, unexpectedly the outer membrane protein A (OmpA) was shown to bind PhoN2-HA through its periplasmic-exposed C-terminal domain. Therefore, to identify PhoN2 domains involved in its periplasmic polar delivery as well as in the interaction with OmpA, a deletion and a set of specific amino acid substitutions were generated. Analysis of these mutants indicated that neither the (183)PAPAP(187) motif of OmpA, nor the N-terminal polyproline (43)PPPP(46) motif and the Y155 residue of PhoN2 are involved in this interaction while P45, P46 and Y155 residues were found to be critical for the correct folding and stability of the protein. The relative rapid degradation of these amino acid-substituted recombinant proteins was found to be due to unknown S. flexneri-specific protease(s). A model depicting how the PhoN2-OmpA interaction may contribute to proper polar IcsA exposition in S. flexneri is presented.
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