ArticleNature communications2023
Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Structures of the Xcp and Hxc T2SS endopili provide new insights into type IV pili subfamilies.Structure (London, England : 1993) · 2026Article
- Insight into the relationship between type IV pilus function and biofilm formation.Biochemical Society transactions · 2026Review
- Visualization of Type IV Pili: Linking Structural Architecture, Dynamic Function, and Translational Opportunities.Biology · 2026Review
- Stimulation of themBio · 2025Article
- Article
- Cryo-EM reconstruction of helical polymers: Beyond the simple cases.Quarterly reviews of biophysics · 2024Review
- Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus.PLoS pathogens · 2024Article
- Saccharibacteria deploy two distinct Type IV pili, driving episymbiosis, host competition, and twitching motility.bioRxiv : the preprint server for biology · 2024Article
- Tight-packing of large pilin subunits provides distinct structural and mechanical properties for theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Semantic segmentation-based detection algorithm for challenging cryo-electron microscopy RNP samples.Frontiers in molecular biosciences · 2024Article
- Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy (cryo-EM) led to structures of several T4F, revealing that the long N-terminal α-helix (α1) - the trademark of pilins - packs in the centre of the filaments to form a hydrophobic core. In diderm bacteria - all available bacterial T4F structures are from diderm species - a portion of α1 is melted (unfolded). Here we report that this architecture is conserved in phylogenetically distant monoderm species by determining the structure of Streptococcus sanguinis T4P. Our 3.7 Å resolution cryo-EM structure of S. sanguinis heteropolymeric T4P and the resulting full atomic model including all minor pilins highlight universal features of bacterial T4F and have widespread implications in understanding T4F biology.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.