ArticleJournal of virology2012
Interactions of the cytoplasmic domain of Sindbis virus E2 with nucleocapsid cores promote alphavirus budding.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
35 citing papers in PubMed, 50 citations in OpenAlex.
- The pathogenicity and virulence of Sindbis virus.Virulence · 2026Review
- Structural and Functional Hallmarks of Sindbis Virus Proteins: From Virion Architecture to Pathogenesis.International journal of molecular sciences · 2025Review
- Current perspectives on alphavirus encapsidation, assembly and budding.Frontiers in cellular and infection microbiology · 2025Review
- Cryogenic electron microscopy and tomography reveal imperfect icosahedral symmetry in alphaviruses.PNAS nexus · 2024Article
- The E2 glycoprotein holds key residues for Mayaro virus adaptation to the urban Aedes aegypti mosquito.PLoS pathogens · 2023Article
- Requirement of a functional ion channel for Sindbis virus glycoprotein transport, CPV-II formation, and efficient virus budding.PLoS pathogens · 2022Article
- Review
- Visualization of conformational changes and membrane remodeling leading to genome delivery by viral class-II fusion machinery.Nature communications · 2022Article
- Chikungunya virus assembly and budding visualized in situ using cryogenic electron tomography.Nature microbiology · 2022Article
- Mutations at the Alphavirus E1'-E2 Interdimer Interface Have Host-Specific Phenotypes.Journal of virology · 2022Article
- Small Molecule Inhibitors Targeting Chikungunya Virus.Current topics in microbiology and immunology · 2022Review
- Capsid-E2 Interactions Rescue Core Assembly in Viruses That Cannot Form Cytoplasmic Nucleocapsid Cores.Journal of virology · 2021Article
- Alphavirus-Induced Membrane Rearrangements during Replication, Assembly, and Budding.Pathogens (Basel, Switzerland) · 2021Review
- ArthritogenicLife (Basel, Switzerland) · 2021Review
- Removing the Polyanionic Cargo Requirement for Assembly of Alphavirus Core-Like Particles to Make an Empty Alphavirus Core.Viruses · 2020Article
- Review
- The Alphavirus E2 Membrane-Proximal Domain Impacts Capsid Interaction and Glycoprotein Lattice Formation.Journal of virology · 2019Article
- Review
- Review
- AnmBio · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Alphavirus budding from the plasma membrane occurs through the specific interaction of the nucleocapsid core with the cytoplasmic domain of the E2 glycoprotein (cdE2). Structural studies of the Sindbis virus capsid protein (CP) have suggested that these critical interactions are mediated by the binding of cdE2 into a hydrophobic pocket in the CP. Several molecular genetic studies have implicated amino acids Y400 and L402 in cdE2 as important for the budding of alphaviruses. In this study, we characterized the role of cdE2 residues in structural polyprotein processing, glycoprotein transport, and capsid interactions. Along with hydrophobic residues, charged residues in the N terminus of cdE2 were critical for the effective interaction of cores with cdE2, a process required for virus budding. Mutations in the C-terminal signal sequence region of cdE2 affected E2 protein transport to the plasma membrane, while nonbudding mutants that were defective in cdE2-CP interaction accumulated E2 on the plasma membrane. The interaction of cdE2 with cytoplasmic cores purified from infected cells and in vitro-assembled core-like particles suggests that cdE2 interacts with assembled cores to mediate budding. We hypothesize that these cdE2 interactions induce a change in the organization of the nucleocapsid core upon binding leading to particle budding and priming of the nucleocapsid cores for disassembly that is required for virus infection.
Indexed as
Identifiers
What OpenQuestion holds
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.