ArticleJournal of bacteriology2013
PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
67 citing papers in PubMed, 114 citations in OpenAlex.
- Article
- Article
- Structural insights into the Thermus thermophilus type IV pilus machinery assembling two distinct pili.Communications biology · 2026Article
- Identifying Pathoadaptation inACS sensors · 2026Article
- A multilayered cell envelope of a member of the Chloroflexota offers an anchoring platform for the archaellum.Frontiers in microbiology · 2026Article
- Proteomic Analysis of the Differential Response ofAntibiotics (Basel, Switzerland) · 2025Article
- Separation ofmBio · 2025Article
- Structure of a functional archaellum in Bacteria of the Chloroflexota phylum.Nature microbiology · 2025Article
- Phage provoke growth delays and SOS response induction despite CRISPR-Cas protection.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- Architectural dissection of adhesive bacterial cell surface appendages from a "molecular machines" viewpoint.Journal of bacteriology · 2024Review
- Type IV pili ofEcoSal Plus · 2024Review
- PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa.Nature communications · 2024Article
- Article
- Analysis ofbioRxiv : the preprint server for biology · 2023Article
- Mechanisms of Antibiotic and Biocide Resistance That Contribute toBiomedicines · 2023Review
- Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).Microbiology (Reading, England) · 2023Review
- Pseudomonas aeruginosa Promotes Persistence of Stenotrophomonas maltophilia via Increased Adherence to Depolarized Respiratory Epithelium.Microbiology spectrum · 2023Article
- Article
- Complete functional analysis of type IV pilus components of a reemergent plant pathogen reveals neofunctionalization of paralog genes.PLoS pathogens · 2023Article
- Characterization of a soluble library of themicroLife · 2023Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Pseudomonas aeruginosa type IV pili (T4P) are virulence factors that promote infection of cystic fibrosis and immunosuppressed patients. As the absence of T4P impairs colonization, they are attractive targets for the development of novel therapeutics. Genes in the pilMNOPQ operon are important for both T4P assembly and a form of bacterial movement, called twitching motility, that is required for pathogenicity. The type II membrane proteins, PilN and PilO, dimerize via their periplasmic domains and anchor this complex in the inner membrane. Our earlier work showed that PilNO binds PilP, a periplasmic lipoprotein (S. Tammam, L. M. Sampaleanu, J. Koo, P. Sundaram, M. Ayers, P. A. Chong, J. D. Forman-Kay, L. L. Burrows, and P. L. Howell, Mol. Microbiol. 82:1496-1514, 2011). Here, we show that PilP interacts with the N0 segment of the outer membrane secretin PilQ via its C-terminal domain, and that the N-terminal cytoplasmic tail of PilN binds to the actin-like protein PilM, thereby connecting all cellular compartments via the PilMNOPQ protein interaction network. We show that PilA, the major pilin subunit, interacts with PilNOPQ. The results allow us to propose a model whereby PilA makes extensive contacts with the transenvelope complex, possibly to increase local concentrations of PilA monomers for polymerization. The PilNOP complex could provide a stable anchor in the inner membrane, while the PilMNOPQ transenvelope complex facilitates transit of the pilus through the periplasm and clamps the pilus in the cell envelope. The PilMN interaction is proposed to be responsible for communicating signals from the cytoplasmic to periplasmic components of this complex macromolecular machine.
Indexed as
Identifiers
What OpenQuestion holds
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.