ArticleRNA (New York, N.Y.)2004
Sindbis virus nucleocapsid assembly: RNA folding promotes capsid protein dimerization.
Article in RNA (New York, N.Y.), 2004. 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, 49 citations in OpenAlex.
- Capsid protein mediated evasion of IRAK1-dependent signalling is essential to Sindbis virus neuroinvasion and virulence in mice.Emerging microbes & infections · 2024Article
- Article
- Small Molecule Inhibitors Targeting Chikungunya Virus.Current topics in microbiology and immunology · 2022Review
- The Structural Biology of Eastern Equine Encephalitis Virus, an Emerging Viral Threat.Pathogens (Basel, Switzerland) · 2021Review
- The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA.Nature communications · 2021Article
- Geometric architecture of viruses.World journal of virology · 2020Review
- Removing the Polyanionic Cargo Requirement for Assembly of Alphavirus Core-Like Particles to Make an Empty Alphavirus Core.Viruses · 2020Article
- Using barcoded Zika virus to assess virus population structure in vitro and in Aedes aegypti mosquitoes.Virology · 2018Article
- The Interplay of Viral and Host Factors in Chikungunya Virus Infection: Targets for Antiviral Strategies.Viruses · 2018Review
- Length of encapsidated cargo impacts stability and structure of in vitro assembled alphavirus core-like particles.Journal of physics. Condensed matter : an Institute of Physics journal · 2017Article
- Identification of Interactions between Sindbis Virus Capsid Protein and Cytoplasmic vRNA as Novel Virulence Determinants.PLoS pathogens · 2017Article
- A novel system for visualizing alphavirus assembly.Journal of virological methods · 2015Article
- Dominance effects of deleterious and beneficial mutations in a single gene of the RNA virus ϕ6.PloS one · 2014Article
- Article
- Probing the early temporal and spatial interaction of the Sindbis virus capsid and E2 proteins with reverse genetics.Journal of virology · 2012Article
- Article
- Interactions of the cytoplasmic domain of Sindbis virus E2 with nucleocapsid cores promote alphavirus budding.Journal of virology · 2012Article
- A structural and functional perspective of alphavirus replication and assembly.Future microbiology · 2009Review
- A five-amino-acid deletion of the eastern equine encephalitis virus capsid protein attenuates replication in mammalian systems but not in mosquito cells.Journal of virology · 2008Article
- Role of sindbis virus capsid protein region II in nucleocapsid core assembly and encapsidation of genomic RNA.Journal of virology · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In Sindbis virus, initiation of nucleocapsid core assembly begins with recognition of the encapsidation signal of the viral RNA genome by capsid protein. This nucleation event drives the recruitment of additional capsid proteins to fully encapsidate the genome, generating an icosahedral nucleocapsid core. The encapsidation signal of the Sindbis virus genomic RNA has previously been localized to a 132-nucleotide region of the genome within the coding region of the nsP1 protein, and the RNA-binding activity of the capsid was previously mapped to a central region of the capsid protein. It is unknown how capsid protein binding to encapsidation signal leads to ordered oligomerization of capsid protein and nucleocapsid core assembly. To address this question, we have developed a mobility shift assay to study this interaction. We have characterized a 32 amino acid peptide capable of recognizing the Sindbis virus encapsidation signal RNA. Using this peptide, we were able to observe a conformational change in the RNA induced by capsid protein binding. Binding is tight (K(d)(app) = 12 nM), and results in dimerization of the capsid peptide. Mutational analysis reveals that although almost every predicted secondary structure within the encapsidation signal is required for efficient protein binding, the identities of the bases within the helices and hairpin turns of the RNA do not need to be maintained. In contrast, two purine-rich loops are essential for binding. From these data, we have developed a model in which the encapsidation signal RNA adopts a highly folded structure and this folding process directs early events in nucleocapsid assembly.
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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.