ArticleVirology2012
Assembly of bacteriophage 80α capsids in a Staphylococcus aureus expression system.
Article in Virology, 2012. 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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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.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Formation and role of the portal ofbioRxiv : the preprint server for biology · 2026Article
- Ribosomal-processing cysteine protease homolog modulatesJournal of bacteriology · 2024Article
- AeLife · 2024Article
- Article
- AbioRxiv : the preprint server for biology · 2023Article
- Phage-Related Ribosomal Protease (Prp) ofBiochemistry · 2022Article
- Shape shifter: redirection of prolate phage capsid assembly by staphylococcal pathogenicity islands.Nature communications · 2021Article
- Staphylococcus epidermidis Phages Transduce Antimicrobial Resistance Plasmids and Mobilize Chromosomal Islands.mSphere · 2021Article
- The gp44 Ejection Protein ofViruses · 2020Article
- Molecular Piracy: Redirection of Bacteriophage Capsid Assembly by Mobile Genetic Elements.Viruses · 2019Review
- Cleavage and Structural Transitions during Maturation of Staphylococcus aureus Bacteriophage 80α and SaPI1 Capsids.Viruses · 2017Article
- Article
- Structural modeling and functional analysis of the essential ribosomal processing protease Prp from Staphylococcus aureus.Molecular microbiology · 2017Article
- Convergent evolution of pathogenicity islands in helper cos phage interference.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016Article
- Specific N-terminal cleavage of ribosomal protein L27 in Staphylococcus aureus and related bacteria.Molecular microbiology · 2015Article
- Pirates of the Caudovirales.Virology · 2012Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
80α is a temperate, double-stranded DNA bacteriophage of Staphylococcus aureus that can act as a "helper" for the mobilization of S. aureus pathogenicity islands (SaPIs), including SaPI1. When SaPI1 is mobilized by 80α, the SaPI genomes are packaged into capsids that are composed of phage proteins, but that are smaller than those normally formed by the phage. This size determination is dependent on SaPI1 proteins CpmA and CpmB. Here, we show that co-expression of the 80α capsid and scaffolding proteins in S. aureus, but not in E. coli, leads to the formation of procapsid-related structures, suggesting that a host co-factor is required for assembly. The capsid and scaffolding proteins also undergo normal N-terminal processing upon expression in S. aureus, implicating a host protease. We also find that SaPI1 proteins CpmA and CpmB promote the formation of small capsids upon co-expression with 80α capsid and scaffolding proteins in S. aureus.
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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.