ArticlePLoS pathogens2024
Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus.
Article in PLoS pathogens, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Disrupting virulence: in silico discovery of MexL inhibitors to block pyocyanin biosynthesis in Pseudomonas aeruginosa.Archives of microbiology · 2026Article
- Structural modeling reveals the mechanism of motor ATPase coordination during type IV pilus retraction.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Isolation of a Novel Lytic Pseudomonas aeruginosa Phage Henu5 and Fitness Costs of Phage-Driven Resistance.Microbial biotechnology · 2026Article
- Role of cell-associated and secretion-independent virulence factors of Pseudomonas aeruginosa in microbial keratitis and anti-virulence therapeutic strategies.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Review
- Article
- Visualization of Type IV Pili: Linking Structural Architecture, Dynamic Function, and Translational Opportunities.Biology · 2026Review
- Exogenous KFrontiers in microbiology · 2026Article
- Separation ofmBio · 2025Article
- Structure of the virulence-associatedProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.Nature communications · 2025Article
- Mapping the ultrastructural topology of the corynebacterial cell surface.PLoS biology · 2025Article
- Architectural dissection of adhesive bacterial cell surface appendages from a "molecular machines" viewpoint.Journal of bacteriology · 2024Review
- The 1.3 Å resolution structure of the truncated group Ia type IV pilin from Pseudomonas aeruginosa strain P1.Acta crystallographica. Section D, Structural biology · 2024Article
- An image processing pipeline for electron cryo-tomography in RELION-5.FEBS open bio · 2024Article
- PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa.Nature communications · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
Type IV pili (T4Ps) are abundant in many bacterial and archaeal species, where they play important roles in both surface sensing and twitching motility, with implications for adhesion, biofilm formation and pathogenicity. While Type IV pilus (T4P) structures from other organisms have been previously solved, a high-resolution structure of the native, fully assembled T4P of Pseudomonas aeruginosa, a major human pathogen, would be valuable in a drug discovery context. Here, we report a 3.2 Å-resolution structure of the P. aeruginosa PAO1 T4P determined by electron cryomicroscopy (cryo-EM). PilA subunits constituting the T4P exhibit a classical pilin fold featuring an extended N-terminal α-helix linked to a C-terminal globular β-sheet-containing domain, which are packed tightly along the pilus, in line with models derived from previous cryo-EM data of the P. aeruginosa PAK strain. The N-terminal helices constitute the pilus core where they stabilise the tubular assembly via hydrophobic interactions. The α-helical core of the pilus is surrounded by the C-terminal globular domain of PilA that coats the outer surface of the pilus, mediating interactions with the surrounding environment. Comparison of the P. aeruginosa PAO1 T4P with T4P structures from other organisms, both at the level of the pilin subunits and the fully assembled pili, confirms previously described common architectural principles whilst highlighting key differences between members of this abundant class of prokaryotic filaments. This study provides a structural framework for understanding the molecular and cell biology of these important cellular appendages mediating interaction of prokaryotes to surfaces.
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