ReviewViruses2020
Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins.
Review in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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.
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Who cites it
35 citing papers in PubMed, 45 citations in OpenAlex.
- Insights into Genome Ejection by a Therapeutic phiKMV-like Bacteriophage.Journal of molecular biology · 2026Article
- Cryo-EM structure of bacteriophage Nocturne116: insights into the architecture of c2-likeJournal of virology · 2026Article
- Structural basis of multimodal adsorption and infection initiation bybioRxiv : the preprint server for biology · 2026Article
- Eco-evolutionary dynamics of massive, parallel bacteriophage outbreaks in compost communities.Science advances · 2026Article
- Characterization and genomic analysis of vB_CoeS_P1, a novel marine bacteriophage, and definition of the new family Estoviridae.Archives of virology · 2026Article
- Structure of defense against restriction proteins DarA and Hdf in phage P1 reveals a new molecular mechanism during phage assembly, infection and DNA ejection.PLoS pathogens · 2026Article
- TheJournal of virology · 2025Article
- Insights into the structure and initial host attachment of the flagellotropic bacteriophage 7-7-1.Communications biology · 2025Article
- Cryo-EM structure of bacteriophage Bas63 reveals structural conservation and diversity in theScience advances · 2025Article
- High-resolution Cryo-EM Analysis of the Therapeutic Pseudomonas Phage Pa223.Journal of molecular biology · 2025Article
- The discovery of aScience advances · 2025Article
- Cryo-EM and cryo-ET reveal the molecular architecture and host interactions of mycobacteriophage Douge.Cell reports · 2025Article
- Article
- Global structural survey of the flagellotropic myophage φTE infecting agricultural pathogen Pectobacterium atrosepticum.Nature communications · 2025Article
- Stabilization mechanism accommodating genome length variation in evolutionarily related viral capsids.Nature communications · 2025Article
- Templated trimerization of the phage L decoration protein on capsids.Protein science : a publication of the Protein Society · 2025Article
- Article
- Article
- The structure of Shigella virus Sf14 reveals the presence of two decoration proteins and two long tail fibers.Communications biology · 2025Article
- Isolation, characterization, and whole-genome analysis of the novel temperate bacteriophage Ph-p5 infecting Glutamicibacter halophytocola.Archives of virology · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Decoration proteins are viral accessory gene products that adorn the surfaces of some phages and viral capsids, particularly tailed dsDNA phages. These proteins often play a "cementing" role, reinforcing capsids against accumulating internal pressure due to genome packaging, or environmental insults such as extremes of temperature or pH. Many decoration proteins serve alternative functions, including target cell recognition, participation in viral assembly, capsid size determination, or modulation of host gene expression. Examples that currently have structures characterized to high-resolution fall into five main folding motifs: β-tulip, β-tadpole, OB-fold, Ig-like, and a rare knotted α-helical fold. Most of these folding motifs have structure homologs in virus and target cell proteins, suggesting horizontal gene transfer was important in their evolution. Oligomerization states of decoration proteins range from monomers to trimers, with the latter most typical. Decoration proteins bind to a variety of loci on capsids that include icosahedral 2-, 3-, and 5-fold symmetry axes, as well as pseudo-symmetry sites. These binding sites often correspond to "weak points" on the capsid lattice. Because of their unique abilities to bind virus surfaces noncovalently, decoration proteins are increasingly exploited for technology, with uses including phage display, viral functionalization, vaccination, and improved nanoparticle design for imaging and drug delivery. These applications will undoubtedly benefit from further advances in our understanding of these versatile augmenters of viral functions.
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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.