ArticleJournal of virology2010
In vitro assembly of the T=13 procapsid of bacteriophage T5 with its scaffolding domain.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- 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
- Structure of the scaffolding protein and portal within the bacteriophage P22 procapsid provides insights into the self-assembly process.PLoS biology · 2025Article
- Phi29 assembly intermediates reveal how scaffold interactions with capsid protein drive capsid construction and maturation.Science advances · 2025Article
- Temperature-induced DNA density transition in phage λ capsid revealed with contrast-matching SANS.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Real-time detection of virus antibody interaction by label-free common-path interferometry.Biophysical reports · 2023Article
- Structure ofViruses · 2023Article
- Siphophage 0105phi7-2 ofInternational journal of molecular sciences · 2023Article
- Capsid Structure ofJournal of virology · 2021Article
- Structural transitions during the scaffolding-driven assembly of a viral capsid.Nature communications · 2019Article
- High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid.Scientific reports · 2017Article
- Genes essential for the morphogenesis of the Shiga toxin 2-transducing phage from Escherichia coli O157:H7.Scientific reports · 2016Article
- Correct Assembly of the Bacteriophage T5 Procapsid Requires Both the Maturation Protease and the Portal Complex.Journal of molecular biology · 2016Article
- Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.Virology · 2015Review
- Solid-to-fluid-like DNA transition in viruses facilitates infection.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly.Journal of molecular biology · 2014Article
- Molecular architecture of tailed double-stranded DNA phages.Bacteriophage · 2014Review
- Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components.Journal of virology · 2014Article
- Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped fibre.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- DNA bending-induced phase transition of encapsidated genome in phage λ.Nucleic acids research · 2013Article
- Insights into head-tailed viruses infecting extremely halophilic archaea.Journal of virology · 2013Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The Siphoviridae coliphage T5 differs from other members of this family by the size of its genome (121 kbp) and by its large icosahedral capsid (90 nm), which is organized with T=13 geometry. T5 does not encode a separate scaffolding protein, but its head protein, pb8, contains a 159-residue aminoterminal scaffolding domain (Delta domain) that is the mature capsid. We have deciphered the early events of T5 shell assembly starting from purified pb8 with its Delta domain (pb8p). The self assembly of pb8p is regulated by salt conditions and leads to structures with distinct morphologies. Expanded tubes are formed in the presence of NaCl, whereas Ca(2+) promotes the association of pb8p into contracted tubes and procapsids. Procapsids display an angular organization and 20-nm-long internal radial structures identified as the Delta domain. The T5 head maturation protease pb11 specifically cleaves the Delta domain of contracted and expanded tubes. Ca(2+) is not required for proteolytic activity but for the organization of the Delta domain. Taken together, these data indicate that pb8p carries all of the information in its primary sequence to assemble in vitro without the requirement of the portal and accessory proteins. Furthermore, Ca(2+) plays a key role in introducing the conformational diversity that permits the formation of a stable procapsid. Phage T5 is the first example of a viral capsid consisting of quasi-equivalent hexamers and pentamers whose assembly can be carried out in vitro, starting from the major head protein with its scaffolding domain, and whose endpoint is an icosahedral T=13 particle.
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