ArticleViruses2022
Evolution of Phage Tail Sheath Protein.
Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 18 citations in OpenAlex.
- Innovative Applications of Artificial Intelligence in Bacteriophage Research: A New Chapter in Future Medicine.Microorganisms · 2026Review
- Metagenomic analysis of the human gut virome reveals functional signatures and viral stability across hospitalized and non-hospitalized diarrheal and non-diarrheal individuals.Gut pathogens · 2026Article
- Genomic, Evolutionary and Phenotypic Insights intoViruses · 2025Article
- Genomic analysis of3 Biotech · 2025Article
- Article
- Global structural survey of the flagellotropic myophage φTE infecting agricultural pathogen Pectobacterium atrosepticum.Nature communications · 2025Article
- Viral Genome Delivery Across Bacterial Cell Surfaces.Annual review of microbiology · 2024Review
- Origin, Evolution and Diversity of φ29-like Phages-Review and Bioinformatic Analysis.International journal of molecular sciences · 2024Review
- NewInternational journal of molecular sciences · 2024Article
- Characterisation of NewViruses · 2024Article
- Article
- Nanotubes from bacteriophage tail sheath proteins: internalisation by cancer cells and macrophages.Nanoscale advances · 2023Article
- Virulent Phage vB_EfaS_WH1 RemovesViruses · 2023Article
- Using AlphaFold Predictions in Viral Research.Current issues in molecular biology · 2023Review
- Prophage-Derived Regions inInternational journal of molecular sciences · 2023Article
- Use of an Integrated Approach Involving AlphaFold Predictions for the Evolutionary Taxonomy ofBiomolecules · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sheath proteins comprise a part of the contractile molecular machinery present in bacteriophages with myoviral morphology, contractile injection systems, and the type VI secretion system (T6SS) found in many Gram-negative bacteria. Previous research on sheath proteins has demonstrated that they share common structural features, even though they vary in their size and primary sequence. In this study, 112 contractile phage tail sheath proteins (TShP) representing different groups of bacteriophages and archaeal viruses with myoviral morphology have been modelled with the novel machine learning software, AlphaFold 2. The obtained structures have been analysed and conserved and variable protein parts and domains have been identified. The common core domain of all studied sheath proteins, including viral and T6SS proteins, comprised both N-terminal and C-terminal parts, whereas the other parts consisted of one or several moderately conserved domains, presumably added during phage evolution. The conserved core appears to be responsible for interaction with the tail tube protein and assembly of the phage tail. Additional domains may have evolved to maintain the stability of the virion or for adsorption to the host cell. Evolutionary relations between TShPs representing distinct viral groups have been proposed using a phylogenetic analysis based on overall structural similarity and other analyses.
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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.