ArticlePLoS pathogens2023
An unbroken network of interactions connecting flagellin domains is required for motility in viscous environments.
Article in PLoS pathogens, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Targeting a conserved flagellin D1 epitope with 16G10 confers cross-serotype protection in murineHuman vaccines & immunotherapeutics · 2026Article
- Structures of the sheathed flagellum reveal mechanisms of assembly and rotation in Vibrio cholerae.Nature microbiology · 2025Article
- Rescue of bacterial motility using two- and three-species FliC chimeras.Journal of bacteriology · 2025Article
- Cryo-EM reconstruction of helical polymers: Beyond the simple cases.Quarterly reviews of biophysics · 2024Review
- Flagellar point mutation causes social aggregation in laboratory-adaptedJournal of bacteriology · 2024Article
- Article
- Two distinct archaeal type IV pili structures formed by proteins with identical sequence.Nature communications · 2024Article
- The evolution of archaeal flagellar filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
In its simplest form, bacterial flagellar filaments are composed of flagellin proteins with just two helical inner domains, which together comprise the filament core. Although this minimal filament is sufficient to provide motility in many flagellated bacteria, most bacteria produce flagella composed of flagellin proteins with one or more outer domains arranged in a variety of supramolecular architectures radiating from the inner core. Flagellin outer domains are known to be involved in adhesion, proteolysis and immune evasion but have not been thought to be required for motility. Here we show that in the Pseudomonas aeruginosa PAO1 strain, a bacterium that forms a ridged filament with a dimerization of its flagellin outer domains, motility is categorically dependent on these flagellin outer domains. Moreover, a comprehensive network of intermolecular interactions connecting the inner domains to the outer domains, the outer domains to one another, and the outer domains back to the inner domain filament core, is required for motility. This inter-domain connectivity confers PAO1 flagella with increased stability, essential for its motility in viscous environments. Additionally, we find that such ridged flagellar filaments are not unique to Pseudomonas but are, instead, present throughout diverse bacterial phyla.
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