Ontology type: schema:ScholarlyArticle Open Access: True
2018-12
AUTHORSMaelenn Chevreuil, Didier Law-Hine, Jingzhi Chen, Stéphane Bressanelli, Sophie Combet, Doru Constantin, Jéril Degrouard, Johannes Möller, Mehdi Zeghal, Guillaume Tresset
ABSTRACTThe survival of viruses partly relies on their ability to self-assemble inside host cells. Although coarse-grained simulations have identified different pathways leading to assembled virions from their components, experimental evidence is severely lacking. Here, we use time-resolved small-angle X-ray scattering to uncover the nonequilibrium self-assembly dynamics of icosahedral viral capsids packaging their full RNA genome. We reveal the formation of amorphous complexes via an en masse pathway and their relaxation into virions via a synchronous pathway. The binding energy of capsid subunits on the genome is moderate (~7kBT0, with kB the Boltzmann constant and T0 = 298 K, the room temperature), while the energy barrier separating the complexes and the virions is high (~ 20kBT0). A synthetic polyelectrolyte can lower this barrier so that filled capsids are formed in conditions where virions cannot build up. We propose a representation of the dynamics on a free energy landscape. More... »
PAGES3071
http://scigraph.springernature.com/pub.10.1038/s41467-018-05426-8
DOIhttp://dx.doi.org/10.1038/s41467-018-05426-8
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1105928848
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/30082710
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"description": "The survival of viruses partly relies on their ability to self-assemble inside host cells. Although coarse-grained simulations have identified different pathways leading to assembled virions from their components, experimental evidence is severely lacking. Here, we use time-resolved small-angle X-ray scattering to uncover the nonequilibrium self-assembly dynamics of icosahedral viral capsids packaging their full RNA genome. We reveal the formation of amorphous complexes via an en masse pathway and their relaxation into virions via a synchronous pathway. The binding energy of capsid subunits on the genome is moderate (~7kBT0, with kB the Boltzmann constant and T0\u2009=\u2009298\u2009K, the room temperature), while the energy barrier separating the complexes and the virions is high (~\u200920kBT0). A synthetic polyelectrolyte can lower this barrier so that filled capsids are formed in conditions where virions cannot build up. We propose a representation of the dynamics on a free energy landscape.",
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"https://doi.org/10.1038/s41467-018-05426-8",
"https://app.dimensions.ai/details/publication/pub.1105928848"
],
"sdDataset": "articles",
"sdDatePublished": "2019-04-10T20:55",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-uberresearch-data-dimensions-target-20181106-alternative/cleanup/v134/2549eaecd7973599484d7c17b260dba0a4ecb94b/merge/v9/a6c9fde33151104705d4d7ff012ea9563521a3ce/jats-lookup/v90/0000000001_0000000264/records_8684_00000567.jsonl",
"type": "ScholarlyArticle",
"url": "https://www.nature.com/articles/s41467-018-05426-8"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
JSON-LD is a popular format for linked data which is fully compatible with JSON.
curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/s41467-018-05426-8'
N-Triples is a line-based linked data format ideal for batch operations.
curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/s41467-018-05426-8'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/s41467-018-05426-8'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/s41467-018-05426-8'
This table displays all metadata directly associated to this object as RDF triples.
293 TRIPLES
21 PREDICATES
79 URIs
21 LITERALS
9 BLANK NODES