ArticleNature communications2019
Structural basis for the adsorption of a single-stranded RNA bacteriophage.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 56 citations in OpenAlex.
- A reference genome without a virus: cDNA reconstruction reveals the provenance and function of the MS2 phage sequence.bioRxiv : the preprint server for biology · 2026Article
- Genome-wide characterization of host factors involved in single-stranded RNA and DNA phage infection pathways.bioRxiv : the preprint server for biology · 2026Article
- The cryo-EM structure of bacteriophage PRR1 and its role in conjugation inhibition.Journal of virology · 2026Article
- Packaging of Single-Stranded RNA in Viruses and Virus-Like Particles.Annual review of biochemistry · 2026Review
- Suppressing Transfer of Antibiotic Resistance by a Small RNA Virus.bioRxiv : the preprint server for biology · 2026Article
- Nanopore direct RNA sequencing (DRS) of MS2 bacteriophages in E. coli throughout its life cycles reveals a complex transcriptional activity to control and maintain its growth.Virology journal · 2026Article
- Review
- Carboxyl-Terminal Region of the Maturation Protein of RNA Coliphage Qβ Mediates Host Attachment, Virion Formation, and Cell Lysis.Genes to cells : devoted to molecular & cellular mechanisms · 2026Article
- Zoo gut plastispheres enable pathogen escape and adaptation.The ISME journal · 2026Article
- Extracellular uncoating of bacteriophage MS2.Journal of molecular biology · 2025Article
- Type IV secretion systems: from structures to mechanisms.The EMBO journal · 2025Review
- Unravelling the dynamics of the maturation protein in MS2 bacteriophage via molecular simulations.Scientific reports · 2025Article
- Viral Genome Delivery Across Bacterial Cell Surfaces.Annual review of microbiology · 2024Review
- Host Receptor Pili for Cryo-EM Single-Particle Reconstruction.Bio-protocol · 2024Article
- Removal ofScience (New York, N.Y.) · 2024Article
- Structural basis of Acinetobacter type IV pili targeting by an RNA virus.Nature communications · 2024Article
- Bacteriophage Receptor Recognition and Nucleic Acid Transfer.Sub-cellular biochemistry · 2024Review
- Purification of Single-Stranded RNA Bacteriophages and Host Receptors for Structural Determination Using Cryo-Electron Microscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Review
- Characterization of the Attachment of Three New Coliphages onto the Ferrichrome Transporter FhuA.Journal of virology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Single-stranded RNA bacteriophages (ssRNA phages) infect Gram-negative bacteria via a single maturation protein (Mat), which attaches to a retractile pilus of the host. Here we present structures of the ssRNA phage MS2 in complex with the Escherichia coli F-pilus, showing a network of hydrophobic and electrostatic interactions at the Mat-pilus interface. Moreover, binding of the pilus induces slight orientational variations of the Mat relative to the rest of the phage capsid, priming the Mat-connected genomic RNA (gRNA) for its release from the virions. The exposed tip of the attached Mat points opposite to the direction of the pilus retraction, which may facilitate the translocation of the gRNA from the capsid into the host cytosol. In addition, our structures determine the orientation of the assembled F-pilin subunits relative to the cell envelope, providing insights into the F-like type IV secretion systems.
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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.