ArticleJournal of molecular biology2012
Structure of the Vibrio cholerae Type IVb Pilus and stability comparison with the Neisseria gonorrhoeae type IVa pilus.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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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Who cites it
45 citing papers in PubMed, 67 citations in OpenAlex.
- Sources of non-Arrhenius electron transport in bacterial nanowires.Physical chemistry chemical physics : PCCP · 2026Article
- Genomic characterization of Comamonas kerstersii isolated from diarrheal patients in Bangladesh.PloS one · 2026Article
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Building permits-control of type IV pilus assembly by PilB and its cofactors.Journal of bacteriology · 2024Review
- Type IV pili ofEcoSal Plus · 2024Review
- Understanding a Core Pilin of the Type IVa Pili ofJournal of microbiology and biotechnology · 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
- Structural basis for the toxin-coregulated pilus-dependent secretion ofScience advances · 2022Article
- The Type IV Pilus of Plasmid TP114 Displays Adhesins Conferring Conjugation Specificity and Is Important for DNA Transfer in the Mouse Gut Microbiota.Microbiology spectrum · 2022Article
- Protein nanowires with tunable functionality and programmable self-assembly using sequence-controlled synthesis.Nature communications · 2022Article
- Motor-independent retraction of type IV pili is governed by an inherent property of the pilus filament.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The minor pilin PilV provides a conserved adhesion site throughout the antigenically variable meningococcal type IV pilus.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- The Role of Minor Pilins in Assembly and Function of the Competence Pilus ofFrontiers in cellular and infection microbiology · 2021Article
- More than a feeling: microscopy approaches to understanding surface-sensing mechanisms.Journal of bacteriology · 2020Review
- Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.Nature communications · 2020Article
- Article
- TheThe Journal of biological chemistry · 2019Article
- Type IV pili: dynamics, biophysics and functional consequences.Nature reviews. Microbiology · 2019Review
- Direct Extracellular Electron Transfer of theBioMed research international · 2019Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Type IV pili are multifunctional filaments displayed on many bacterial pathogens. Members of the Type IVa pilus subclass are found on a diverse group of human pathogens, whereas Type IVb pili are found almost exclusively on enteric bacteria. The Type IVa and IVb subclasses are distinguished by differences in the pilin subunits, including the fold of the globular domain. To understand the implications of the distinct pilin folds, we compared the stabilities of pilin subunits and pilus filaments for the Type IVa GC pilus from Neisseria gonorrhoeae and the Type IVb toxin-coregulated pilus (TCP) from Vibrio cholerae. We show that while recombinant TCP pilin is more stable than GC pilin, the GC pili are more resistant to proteolysis, heat and chemical denaturation than TCP, remaining intact in 8 M urea. To understand these differences, we determined the TCP structure by electron microscopy and three-dimensional image reconstruction. TCP have an architecture similar to that of GC pili, with subunits arranged in a right-handed 1-start helix and related by an 8.4-Å axial rise and a 96.8° azimuthal rotation. However, the TCP subunits are not as tightly packed as GC pilins, and the distinct Type IVb pilin fold exposes a segment of the α-helical core of TCP. Hydrophobic interactions dominate for both pilus subtypes, but base stacking by aromatic residues conserved among the Type IVa pilins may contribute to GC pilus stability. The extraordinary stability of GC pili may represent an adaptation of the Type IVa pili to harsh environments and the need to retract against external forces.
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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.