ArticleJournal of virology2008
Bluetongue virus outer capsid protein VP5 interacts with membrane lipid rafts via a SNARE domain.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 54 citations in OpenAlex.
- A Molecular and Structural Perspective on Bluetongue Virus Entry and Assembly.Pathogens (Basel, Switzerland) · 2026Review
- Glycosylated NS3/NS3A protein of bluetongue virus facilitates efficient viral egress via lipid raft anchoring.Journal of virology · 2026Article
- Insect-borne non-enveloped bluetongue virus utilizes discrete small vesicles for non-lytic release and cell-to-cell transmission.PLoS pathogens · 2025Article
- Immuno-informatics study identifies conserved T cell epitopes in non-structural proteins of Bluetongue virus serotypes: formulation of a computationally optimized next-generation broad-spectrum multi-epitope vaccine.Frontiers in immunology · 2024Article
- Human Papillomavirus Minor Capsid Protein L2 Mediates Intracellular Trafficking into and Passage beyond the Endoplasmic Reticulum.Microbiology spectrum · 2022Article
- Bluetongue virus capsid protein VP5 perforates membranes at low endosomal pH during viral entry.Nature microbiology · 2021Article
- Structural Domains of the Herpes Simplex Type 1 gD Protein that Restrict HIV-1 Particle Infectivity.Journal of virology · 2021Article
- Multiple Routes of Bluetongue Virus Egress.Microorganisms · 2020Review
- Differential Localization of Structural and Non-Structural Proteins during the Bluetongue Virus Replication Cycle.Viruses · 2020Article
- Bluetongue virus assembly and exit pathways.Advances in virus research · 2020Review
- Bluetongue Virus Nonstructural Protein 3 Orchestrates Virus Maturation and Drives Non-Lytic Egress via Two Polybasic Motifs.Viruses · 2019Article
- Novel Function of Bluetongue Virus NS3 Protein in Regulation of the MAPK/ERK Signaling Pathway.Journal of virology · 2019Article
- Review
- Unraveling the role of membrane microdomains during microbial infections.Cell biology and toxicology · 2017Review
- Structural Protein VP2 of African Horse Sickness Virus Is Not Essential for Virus Replication In Vitro.Journal of virology · 2017Article
- Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry.Nature structural & molecular biology · 2016Article
- Interactions between cyclodextrins and cellular components: Towards greener medical applications?Beilstein journal of organic chemistry · 2016Review
- Turnover Rate of NS3 Proteins Modulates Bluetongue Virus Replication Kinetics in a Host-Specific Manner.Journal of virology · 2015Article
- Influence of cellular trafficking pathway on bluetongue virus infection in ovine cells.Viruses · 2015Article
- Multiple genome segments determine virulence of bluetongue virus serotype 8.Journal of virology · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bluetongue virus (BTV) is a nonenveloped double-stranded RNA virus belonging to the family Reoviridae. The two outer capsid proteins, VP2 and VP5, are responsible for virus entry. However, little is known about the roles of these two proteins, particularly VP5, in virus trafficking and assembly. In this study, we used density gradient fractionation and methyl beta cyclodextrin, a cholesterol-sequestering drug, to demonstrate not only that VP5 copurifies with lipid raft domains in both transfected and infected cells, but also that raft domain integrity is required for BTV assembly. Previously, we showed that BTV nonstructural protein 3 (NS3) interacts with VP2 and also with cellular exocytosis and ESCRT pathway proteins, indicating its involvement in virus egress (A. R. Beaton, J. Rodriguez, Y. K. Reddy, and P. Roy, Proc. Natl. Acad. Sci. USA 99:13154-13159, 2002; C. Wirblich, B. Bhattacharya, and P. Roy J. Virol. 80:460-473, 2006). Here, we show by pull-down and confocal analysis that NS3 also interacts with VP5. Further, a conserved membrane-docking domain similar to the motif in synaptotagmin, a protein belonging to the SNARE (soluble N-ethylmaleimide-sensitive fusion attachment protein receptor) family was identified in the VP5 sequence. By site-directed mutagenesis, followed by flotation and confocal analyses, we demonstrated that raft association of VP5 depends on this domain. Together, these results indicate that VP5 possesses an autonomous signal for its membrane targeting and that the interaction of VP5 with membrane-associated NS3 might play an important role in virus 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.