ArticleNature communications2025
The structure of the Tad pilus alignment complex reveals a periplasmic conduit for pilus extension.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Article
- Multi-omics characterization of β-myrcene-evolvedFrontiers in molecular biosciences · 2026Article
- Comparative proteomics reveals hydrogenase-centered steel-dependent growth and corrosion inFrontiers in microbiology · 2026Article
- Article
- Characterization and Genomic Analysis ofAnimals : an open access journal from MDPI · 2025Article
- Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025Article
- Conformational changes in the motor ATPase CpaF facilitate a rotary mechanism of Tad pilus assembly.Nature communications · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The Tad (Tight adherence) pilus is a bacterial appendage implicated in virulence, cell-cell aggregation, and biofilm formation. Despite its homology to the well-characterised Type IV pilus, the structure and assembly mechanism of the Tad pilus are poorly understood. Here, we investigate the role of the Tad pilus protein RcpC from Pseudomonas aeruginosa. Our analyses reveal that RcpC forms a dodecameric periplasmic complex, anchored to the inner membrane by a transmembrane helix, and interacting with the outer membrane secretin RcpA. We use single-particle Cryo-EM to elucidate the structure of the RcpC dodecamer, and cell-based assays to demonstrate that the RcpC-RcpA complex is essential for Tad-mediated cell-cell aggregation. Collectively, these data demonstrate that RcpC forms the Tad pilus alignment complex, which provides a conduit across the periplasm for the Tad pilus filament to access the extracellular milieu. Our experimental data and structure-based model allow us to propose a mechanism for Tad plus assembly.
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Registered trials
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