ArticleFrontiers in molecular biosciences2022
A structural discovery journey of streptococcal phages adhesion devices by AlphaFold2.
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Article
- Diversity and prevalence of dairy streptococcal phages in two European dairy fermentation facilities over a one-year period.Microbial genomics · 2026Article
- From CASP13 to the Nobel Prize: DeepMind's AlphaFold Journey in Revolutionizing Protein Structure Prediction and Beyond.Current protein & peptide science · 2026Review
- Predicted Structures ofViruses · 2025Article
- Characterization of strictly lytic phages infectingMicrobiology spectrum · 2025Article
- AlphaFold 3: an unprecedent opportunity for fundamental research and drug development.Precision clinical medicine · 2025Review
- Isolation of phages infecting the zoonotic pathogenbioRxiv : the preprint server for biology · 2025Article
- Deciphering the adsorption machinery of Deep-Blue and Vp4, two myophages targeting members of theJournal of virology · 2024Article
- Article
- Partial Atomic Model of the Tailed Lactococcal Phage TP901-1 as Predicted by AlphaFold2: Revelations and Limitations.Viruses · 2023Article
- Bacteriophage-host interactions in Streptococcus thermophilus and their impact on co-evolutionary processes.FEMS microbiology reviews · 2023Review
- Insights into theInternational journal of molecular sciences · 2023Article
- Exploring Host-Binding Machineries of Mycobacteriophages with AlphaFold2.Journal of virology · 2023Article
- AlphaFold2 and its applications in the fields of biology and medicine.Signal transduction and targeted therapy · 2023Review
- Phage Adsorption to Gram-Positive Bacteria.Viruses · 2023Review
- Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2.Microorganisms · 2022Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Successful bacteriophage infection starts with specific recognition and adhesion to the host cell surface. Adhesion devices of siphophages infecting Gram-positive bacteria are very diverse and remain, for the majority, poorly understood. These assemblies often comprise long, flexible, and multi-domain proteins, which limits their structural analyses by experimental approaches such as X-ray crystallography and electron microscopy. However, the protein structure prediction program AlphaFold2 is exquisitely adapted to unveil structural and functional details of such molecular machineries. Here, we present structure predictions of whole adhesion devices of five representative siphophages infecting
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