ArticleVirology2014
Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain.
Article in Virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 31 citations in OpenAlex.
- TheJournal of virology · 2025Article
- Moo19 and B2: Structures ofScience advances · 2024Article
- The Structural Diversity of Encapsulin Protein Shells.Chembiochem : a European journal of chemical biology · 2024Review
- Bacteriophages: sustainable and effective solution for climate-resilient agriculture.Sustainable microbiology · 2024Review
- A Capsid Structure ofViruses · 2022Article
- Predicting the capsid architecture of phages from metagenomic data.Computational and structural biotechnology journal · 2022Article
- The Missing Tailed Phages: Prediction of Small Capsid Candidates.Microorganisms · 2020Article
- Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages.Journal of virology · 2019Article
- The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.eLife · 2019Article
- Biological Applications at the Cutting Edge of Cryo-Electron Microscopy.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2018Review
- Shigella Phages Isolated during a Dysentery Outbreak Reveal Uncommon Structures and Broad Species Diversity.Journal of virology · 2018Article
- Review
- NMR assignments for the insertion domain of bacteriophage Sf6 coat protein.Biomolecular NMR assignments · 2017Article
- Contributions of P2- and P22-like prophages to understanding the enormous diversity and abundance of tailed bacteriophages.Virology · 2016Article
- Article
- An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology.Methods (San Diego, Calif.) · 2016Article
- Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Biophysical journal · 2015Article
- NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.Biomolecular NMR assignments · 2015Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Bacteriophage lambda: Early pioneer and still relevant.Virology · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
CUS-3 is a short-tailed, dsDNA bacteriophage that infects serotype K1 Escherichia coli. We report icosahedrally averaged and asymmetric, three-dimensional, cryo-electron microscopic reconstructions of the CUS-3 virion. Its coat protein structure adopts the "HK97-fold" shared by other tailed phages and is quite similar to that in phages P22 and Sf6 despite only weak amino acid sequence similarity. In addition, these coat proteins share a unique extra external domain ("I-domain"), suggesting that the group of P22-like phages has evolved over a very long time period without acquiring a new coat protein gene from another phage group. On the other hand, the morphology of the CUS-3 tailspike differs significantly from that of P22 or Sf6, but is similar to the tailspike of phage K1F, a member of the extremely distantly related T7 group of phages. We conclude that CUS-3 obtained its tailspike gene from a distantly related phage quite recently.
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.