ArticleJournal of bacteriology2005
Agrobacterium tumefaciens VirB9, an outer-membrane-associated component of a type IV secretion system, regulates substrate selection and T-pilus biogenesis.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 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
56 citing papers in PubMed, 89 citations in OpenAlex.
- Article
- Contributions of conserved and species-specific CagX (VirB9) domains to the assembly and function of theInfection and immunity · 2026Article
- Type IV Secretion System Drives Lipid Mixing.bioRxiv : the preprint server for biology · 2026Article
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- The R plasmid pRAS2 in the fish pathogenFrontiers in microbiology · 2026Article
- Article
- Structural and functional diversity of type IV secretion systems.Nature reviews. Microbiology · 2024Review
- Chimeric systems composed of swapped Tra subunits between distantly-related F plasmids reveal striking plasticity among type IV secretion machines.PLoS genetics · 2024Article
- Cryo-EM structure of the Agrobacterium tumefaciens T4SS-associated T-pilus reveals stoichiometric protein-phospholipid assembly.Structure (London, England : 1993) · 2023Article
- Structure of a type IV secretion system core complex encoded by multi-drug resistance F plasmids.Nature communications · 2022Article
- Type IV secretion systems: Advances in structure, function, and activation.Molecular microbiology · 2021Review
- Article
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
- Characterization of a Novel Diarrheagenic Strain ofFrontiers in microbiology · 2019Article
- The role of integrating conjugative elements in Helicobacter pylori: a review.Journal of biomedical science · 2018Review
- Phylogeographic diversity and mosaicism of theMobile DNA · 2018Article
- Substrate translocation involves specific lysine residues of the central channel of the conjugative coupling protein TrwB.Molecular genetics and genomics : MGG · 2017Article
- Use of chimeric type IV secretion systems to define contributions of outer membrane subassemblies for contact-dependent translocation.Molecular microbiology · 2017Article
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Agrobacterium tumefaciens translocates DNA and protein substrates between cells via a type IV secretion system (T4SS) whose channel subunits include the VirD4 coupling protein, VirB11 ATPase, VirB6, VirB8, VirB2, and VirB9. In this study, we used linker insertion mutagenesis to characterize the contribution of the outer-membrane-associated VirB9 to assembly and function of the VirB/D4 T4SS. Twenty-five dipeptide insertion mutations were classified as permissive for intercellular substrate transfer (Tra+), completely transfer defective (Tra-), or substrate discriminating, e.g., selectively permissive for transfer only of the oncogenic transfer DNA and the VirE2 protein substrates or of a mobilizable IncQ plasmid substrate. Mutations inhibiting transfer of DNA substrates did not affect formation of close contacts of the substrate with inner membrane channel subunits but blocked formation of contacts with the VirB2 and VirB9 channel subunits, which is indicative of a defect in assembly or function of the distal portion of the secretion channel. Several mutations in the N- and C-terminal regions disrupted VirB9 complex formation with the outer-membrane-associated lipoprotein VirB7 or the inner membrane energy sensor VirB10. Several VirB9.i2-producing Tra+ strains failed to elaborate T pilus at detectable levels (Pil-), and three such Tra+ Pil- mutant strains were rendered Tra- upon deletion of virB2, indicating that the cellular form of pilin protein is essential for substrate translocation. Our findings, together with computer-based analyses, support a model in which distinct domains of VirB9 contribute to substrate selection and translocation, establishment of channel subunit contacts, and T-pilus biogenesis.
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.