ArticleStructure (London, England : 1993)2025
Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein.
Article in Structure (London, England : 1993), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Cryo-EM structure of bacteriophage Nocturne116: insights into the architecture of c2-likeJournal of virology · 2026Article
- Intact architectures of myophage phi92 in extended and contracted states.PLoS pathogens · 2026Article
- Article
- Dynamic adhesion device of phage OE33PA drives Gram-positive host recognition.bioRxiv : the preprint server for biology · 2026Article
- In situ structures of the portal-neck-tail complex of bacteriophage T4 inform a viral genome positioning mechanism.Nature communications · 2026Article
- Formation and role of the portal ofbioRxiv : the preprint server for biology · 2026Article
- Genome anchoring, retention, and release by neck proteins of Staphylococcus phage 812.Communications biology · 2026Article
- TheJournal of virology · 2025Article
- Structural basis of bacteriophage Ur-lambda infection initiation.Science advances · 2025Article
Corrections and comments
- Update ofStructure of the2024
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4 authors.
Funding
Abstract
The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from helper-encoded structural proteins. 80α and SaPI1 virions consist of an icosahedral head connected via a portal vertex to a long, non-contractile tail. A connector or "neck" forms the interface between the tail and the head. Here, we have determined the high-resolution structure of the neck section of SaPI1 virions, including the dodecameric portal and head-tail-connector proteins, and the hexameric head-tail joining, tail terminator and major tail proteins. We also resolved the DNA, the tail completion protein (TCP), and the tape measure protein (TMP) inside the tail, features that have not previously been observed at high resolution. Our study provides insights into the assembly and infection process in this important group of MGEs.
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