ArticleMolecular microbiology2010
Vibrio cholerae El Tor TcpA crystal structure and mechanism for pilus-mediated microcolony formation.
Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 37 citations in OpenAlex.
- Article
- Cryo-Electron Microscopy of BfpB Reveals a Type IVb Secretin Multimer Adapted to Accommodate the Exceptionally Wide Bundle-Forming Pilus.Pathogens (Basel, Switzerland) · 2025Article
- Review
- Article
- A review on pilus assembly mechanisms in Gram-positive and Gram-negative bacteria.Cell surface (Amsterdam, Netherlands) · 2022Article
- InactivatedJournal of microbiology and biotechnology · 2022Article
- Recombinant Globular Domain of TcpA Pilin fromLife (Basel, Switzerland) · 2022Article
- Structural basis for the toxin-coregulated pilus-dependent secretion ofScience advances · 2022Article
- A practical overview of molecular replacement: Clostridioides difficile PilA1, a difficult case study.Acta crystallographica. Section D, Structural biology · 2020Article
- Vibrio Pathogenicity Island-1: The Master Determinant of Cholera Pathogenesis.Frontiers in cellular and infection microbiology · 2020Review
- DNA-uptake pili of Vibrio cholerae are required for chitin colonization and capable of kin recognition via sequence-specific self-interaction.Nature microbiology · 2019Article
- Regulatory Hierarchies Controlling Virulence Gene Expression inFrontiers in microbiology · 2018Review
- Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution.Structure (London, England : 1993) · 2017Article
- The Vibrio cholerae Minor Pilin TcpB Initiates Assembly and Retraction of the Toxin-Coregulated Pilus.PLoS pathogens · 2016Article
- Effects of tcpB Mutations on Biogenesis and Function of the Toxin-Coregulated Pilus, the Type IVb Pilus of Vibrio cholerae.Journal of bacteriology · 2016Article
- Crystal Structure of the Minor Pilin CofB, the Initiator of CFA/III Pilus Assembly in Enterotoxigenic Escherichia coli.The Journal of biological chemistry · 2015Article
- A Genome-Wide Screen Reveals that the Vibrio cholerae Phosphoenolpyruvate Phosphotransferase System Modulates Virulence Gene Expression.Infection and immunity · 2015Article
- The Cpx system regulates virulence gene expression in Vibrio cholerae.Infection and immunity · 2015Article
- High-resolution structure of a type IV pilin from the metal-reducing bacterium Shewanella oneidensis.BMC structural biology · 2015Article
- Predicting Homogeneous Pilus Structure from Monomeric Data and Sparse Constraints.BioMed research international · 2015Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Type IV pili (T4P) are critical to virulence for Vibrio cholerae and other bacterial pathogens. Among their diverse functions, T4P mediate microcolony formation, which protects the bacteria from host defences and concentrates secreted toxins. The T4P of the two V. cholerae O1 disease biotypes, classical and El Tor, share 81% identity in their TcpA subunits, yet these filaments differ in their interaction patterns as assessed by electron microscopy. To understand the molecular basis for pilus-mediated microcolony formation, we solved a 1.5 A resolution crystal structure of N-terminally truncated El Tor TcpA and compared it with that of classical TcpA. Residues that differ between the two pilins are located on surface-exposed regions of the TcpA subunits. By iteratively changing these non-conserved amino acids in classical TcpA to their respective residues in El Tor TcpA, we identified residues that profoundly affect pilus:pilus interaction patterns and bacterial aggregation. These residues lie on either the protruding d-region of the TcpA subunit or in a cavity between pilin subunits in the pilus filament. Our results support a model whereby pili interact via intercalation of surface protrusions on one filament into depressions between subunits on adjacent filaments as a means to hold V. cholerae cells together in microcolonies.
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