ArticleJournal of virology2003
Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed.
- Article
- Multi-Gene Recombinant Baculovirus Expression Systems: From Inception to Contemporary Applications.Viruses · 2024Review
- A multidisciplinary approach to the identification of the protein-RNA connectome in double-stranded RNA virus capsids.Nucleic acids research · 2023Article
- Cryo-electron microscopy for the study of virus assembly.Nature chemical biology · 2020Review
- Bluetongue virus assembly and exit pathways.Advances in virus research · 2020Review
- Bluetongue virus capsid assembly and maturation.Viruses · 2014Review
- The molecular biology of Bluetongue virus replication.Virus research · 2014Review
- On the effect of thermodynamic equilibrium on the assembly efficiency of complex multi-layered virus-like particles (VLP): the case of rotavirus VLP.PLoS computational biology · 2012Article
- Bluetongue virus RNA binding protein NS2 is a modulator of viral replication and assembly.BMC molecular biology · 2007Article
- Virus-like particles: models for assembly studies and foreign epitope carriers.Progress in nucleic acid research and molecular biology · 2005Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The surface of the bluetongue virus core forms a T=13 quasiequivalent icosahedral protein shell with 260 trimers of a single gene product: VP7 protein. Underneath is a smooth layer, made up of VP3 protein, which appears to guide and nucleate the assembly of VP7 trimers. The contacts between the two shells are extensive but nonspecific, and construction of the T=13 icosahedral shell requires polymorphism in the association of the VP7 subunits, each of which has two domains that contribute to trimer formation. We used structural and relative sequence information to guide an investigation of how such a complex structure is achieved during virus assembly and what residues are required to form a stable capsid. Fifteen single or multiple site-specific substitution mutations were introduced into the helical domain of VP7, which is closely associated with the VP3 layer, and the effects on capsid assembly were analyzed. Our data show that both the position and the nature of single residues are critical for the attachment of VP7 to VP3 and that formation of a stable VP7 lattice is not the automatic consequence of trimer formation.
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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.