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individual
rights: termsOfUse
date: 2026-08-26T03:59:37
publisher: vivo
type: Document
label: RDF description of Self-assembly of viral capsid protein and RNA molecules of different sizes: Requirement for a specific high protein/RNA mass: Ratio - http://orbis.uaslp.mx/vivo/individual/scopus3103

Self-assembly of viral capsid protein and RNA molecules of different sizes: Requirement for a specific high protein/RNA mass: Ratio
date time value: article date 3104
type: Thing
related by: authorship_18083
type: Article
related by: authorship_18080
issue: 6
type: Information Content Entity
most specific type: Article
crisid: 3104
accesstype: All Open Access, Bronze, Green
related by: authorship_18082
doi: 10.1128/JVI.06566-11
volume: 86
page end: 3326
freetext keyword: capsid protein; double stranded RNA; nucleotide; single stranded RNA; virus RNA; amino terminal sequence; article; base pairing; controlled study; in vitro study; molecular weight; nonhuman; priority journal; protein assembly; protein RNA binding; RNA gene; RNA structure; RNA transcription; transmission electron microscopy; virus assembly; virus capsid; virus particle; wild type; Bromovirus; Capsid Proteins; Fabaceae; Plant Diseases; RNA, Viral; Virus Assembly; Cowpea chlorotic mottle virus; Miridae
type: Document
e iscopus: 2-s2.0-84857959507
has funding vehicle: National Institute of Allergy and Infectious Diseases, NIAID: R21AI082301
related by: authorship_18079
has publication venue: Journal of Virology
chemicalscas: Capsid Proteins; RNA, Viral
type: Entity
origen: scopus
page start: 3318
pmid: 22205731
related by: authorship_18078
type: Generically Dependent Continuant
related by: authorship_18081
abstract: Virus-like particles can be formed by self-assembly of capsid protein (CP) with RNA molecules of increasing length. If the protein insisted on a single radius of curvature, the capsids would be identical in size, independent of RNA length. However, there would be a limit to length of the RNA, and one would not expect RNA much shorter than native viral RNA to be packaged unless multiple copies were packaged. On the other hand, if the protein did not favor predetermined capsid size, one would expect the capsid diameter to increase with increase in RNA length. Here we examine the self-assembly of CP from cowpea chlorotic mottle virus with RNA molecules ranging in length from 140 to 12,000 nucleotides (nt). Each of these RNAs is completely packaged if and only if the protein/RNA mass ratio is sufficiently high; this critical value is the same for all of the RNAs and corresponds to equal RNA and N-terminal-protein charges in the assembly mix. For RNAs much shorter in length than the 3,000 nt of the viral RNA, two or more molecules are assembled into 24- and 26-nm-diameter capsids, whereas for much longer RNAs (>4,500 nt), a single RNA molecule is shared/packaged by two or more capsids with diameters as large as 30 nm. For intermediate lengths, a single RNA is assembled into 26-nm-diameter capsids, the size associated with T=3 wild-type virus. The significance of these assembly results is discussed in relation to likely factors that maintain T=3 symmetry in vivo. © 2012, American Society for Microbiology.
estado: published
most specific type: Document
type: Continuant

Article
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Journal of Virology
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publication venue for: Self-assembly of viral capsid protein and RNA molecules of different sizes: Requirement for a specific high protein/RNA mass: Ratio
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Information Content Entity
type: Class

National Institute of Allergy and Infectious Diseases, NIAID: R21AI082301
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type: BFO_0000020
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type: Thing
type: Grant
type: Continuant
funding vehicle for: Self-assembly of viral capsid protein and RNA molecules of different sizes: Requirement for a specific high protein/RNA mass: Ratio