ArticleJournal of virology2013
The amino-terminal domain of alphavirus capsid protein is dispensable for viral particle assembly but regulates RNA encapsidation through cooperative functions of its subdomains.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 47 citations in OpenAlex.
- Venezuelan Equine Encephalitis Virus: Structural Biology, Vaccines, and Advances in Functional Antibodies.Vaccines · 2025Review
- Establishment of a Chikungunya virus pseudotype system strictly dependent on viral protein expression.The Journal of general virology · 2025Article
- A detailed kinetic model of Eastern equine encephalitis virus replication in a susceptible host cell.PLoS computational biology · 2025Article
- The sticky business of Alphavirus capsid-host interactions.Trends in microbiology · 2025Review
- Application of Pseudoinfectious Viruses in Transient Gene Expression in Mammalian Cells: Combining Efficient Expression with Regulatory Compliance.Biomolecules · 2025Article
- Current perspectives on alphavirus encapsidation, assembly and budding.Frontiers in cellular and infection microbiology · 2025Review
- Distinct chikungunya virus polymerase palm subdomains contribute to viral protein accumulation and virion production.PLoS pathogens · 2024Article
- The evolutionary and molecular history of a chikungunya virus outbreak lineage.PLoS neglected tropical diseases · 2024Article
- Distinct chikungunya virus polymerase palm subdomains contribute to virus replication and virion assembly.bioRxiv : the preprint server for biology · 2024Article
- Capsid-E2 Interactions Rescue Core Assembly in Viruses That Cannot Form Cytoplasmic Nucleocapsid Cores.Journal of virology · 2021Article
- Semliki Forest Virus Chimeras with Functional Replicase Modules from Related Alphaviruses Survive by Adaptive Mutations in Functionally Important Hot Spots.Journal of virology · 2021Article
- Rediscovering the chikungunya virusBiomedica : revista del Instituto Nacional de Salud · 2021Review
- Cryo-EM structure of the mature and infective Mayaro virus at 4.4 Å resolution reveals features of arthritogenic alphaviruses.Nature communications · 2021Article
- ArthritogenicLife (Basel, Switzerland) · 2021Review
- Article
- Removing the Polyanionic Cargo Requirement for Assembly of Alphavirus Core-Like Particles to Make an Empty Alphavirus Core.Viruses · 2020Article
- Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation.PLoS pathogens · 2020Article
- Insight into the origin of chikungunya virus in Malaysian non-human primates via sequence analysis.Heliyon · 2019Article
- Infectious Chikungunya Virus (CHIKV) with a Complete Capsid Deletion: a New Approach for a CHIKV Vaccine.Journal of virology · 2019Article
- The Alphavirus E2 Membrane-Proximal Domain Impacts Capsid Interaction and Glycoprotein Lattice Formation.Journal of virology · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Venezuelan equine encephalitis virus (VEEV) is a pathogenic alphavirus, which circulates in the Central, South, and North Americas, including the United States, and represents a significant public health threat. In recent years, strong progress has been made in understanding the structure of VEEV virions, but the mechanism of their formation has yet to be investigated. In this study, we analyzed the functions of different capsid-specific domains and its amino-terminal subdomains in viral particle formation. Our data demonstrate that VEEV particles can be efficiently formed directly at the plasma membrane without cytoplasmic nucleocapsid preassembly. The entire amino-terminal domain of VEEV capsid protein was found to be dispensable for particle formation. VEEV variants encoding only the capsid's protease domain efficiently produce genome-free VEEV virus-like particles (VLPs), which are very similar in structure to the wild-type virions. The amino-terminal domain of the VEEV capsid protein contains at least four structurally and functionally distinct subdomains, which mediate RNA packaging and the specificity of packaging in particular. The most positively charged subdomain is a negative regulator of the nucleocapsid assembly. The three other subdomains are not required for genome-free VLP formation but are important regulators of RNA packaging. Our data suggest that the positively charged surface of the VEEV capsid-specific protease domain and the very amino-terminal subdomain are also involved in interaction with viral RNA and play important roles in RNA encapsidation. Finally, we show that VEEV variants with mutated capsid acquire compensatory mutations in either capsid or nsP2 genes.
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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.