ArticleJournal of virology2000
Functional dissection of the major structural protein of bluetongue virus: identification of key residues within VP7 essential for capsid assembly.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Multi-Gene Recombinant Baculovirus Expression Systems: From Inception to Contemporary Applications.Viruses · 2024Review
- A blocking ELISA based on virus-like nanoparticles chimerized with an antigenic epitope of ASFV P54 for detecting ASFV antibodies.Scientific reports · 2023Article
- Generation of a Soluble African Horse Sickness Virus VP7 Protein Capable of Forming Core-like Particles.Viruses · 2022Article
- Bluetongue virus assembly and exit pathways.Advances in virus research · 2020Review
- Review
- Interaction between a Unique Minor Protein and a Major Capsid Protein of Bluetongue Virus Controls Virus Infectivity.Journal of virology · 2018Article
- Bluetongue virus capsid assembly and maturation.Viruses · 2014Review
- The molecular biology of Bluetongue virus replication.Virus research · 2014Review
- Minimum requirements for bluetongue virus primary replication in vivo.Journal of virology · 2013Article
- In vitro reconstitution of Bluetongue virus infectious cores.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Oncolytic bluetongue viruses: promise, progress, and perspectives.Frontiers in microbiology · 2011Article
- Article
- Bluetongue virus outer capsid protein VP5 interacts with membrane lipid rafts via a SNARE domain.Journal of virology · 2008Article
- Rapid identification of known and new RNA viruses from animal tissues.PLoS pathogens · 2008Article
- Interaction between Bluetongue virus outer capsid protein VP2 and vimentin is necessary for virus egress.Virology journal · 2007Article
- Assembly and intracellular localization of the bluetongue virus core protein VP3.Journal of virology · 2005Article
- Virus-like particles: models for assembly studies and foreign epitope carriers.Progress in nucleic acid research and molecular biology · 2005Review
- Role of interfacial amino acid residues in assembly, stability, and conformation of a spherical virus capsid.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Defining the structure-function relationships of bluetongue virus helicase protein VP6.Journal of virology · 2003Article
- Intermolecular interactions in a two-layered viral capsid that requires a complex symmetry mismatch.Journal of virology · 2003Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A lattice of VP7 trimers forms the surface of the icosahedral bluetongue virus (BTV) core. To investigate the role of VP7 oligomerization in core assembly, a series of residues for substitution were predicted based on crystal structures of BTV type 10 VP7 molecule targeting the monomer-monomer contacts within the trimer. Seven site-specific substitution mutations of VP7 have been created using cDNA clones and were employed to produce seven recombinant baculoviruses. The effects of these mutations on VP7 solubility, ability to trimerize and formation of core-like particles (CLPs) in the presence of the scaffolding VP3 protein, were investigated. Of the seven VP7 mutants examined, three severely affected the stability of CLP, while two other mutants had lesser effect on CLP stability. Only one mutant had no apparent effect on the formation of the stable capsid. One mutant in which the conserved tyrosine at residue 271 (lower domain helix 6) was replaced by arginine formed insoluble aggregates, implying an effect in the folding of the molecule despite the prediction that such a change would be accommodated. All six soluble VP7 mutants were purified, and their ability to trimerize was examined. All mutants, including those that did not form stable CLPs, assembled into stable trimers, implying that single substitution may not be sufficient to perturb the complex monomer-monomer contacts, although subtle changes within the VP7 trimer could destabilize the core. The study highlights some of the key residues that are crucial for BTV core assembly and illustrates how the structure of VP7 in isolation underrepresents the dynamic nature of the assembly process at the biological level.
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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.