ArticleJournal of virology2000
Rotavirus spike protein VP4 is present at the plasma membrane and is associated with microtubules in infected cells.
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 35 papers.
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Who cites it
35 citing papers in PubMed, 76 citations in OpenAlex.
- Significance of Cellular Lipid Metabolism for the Replication of Rotaviruses and Other RNA Viruses.Viruses · 2024Review
- The Role of the Host Cytoskeleton in the Formation and Dynamics of Rotavirus Viroplasms.Viruses · 2024Review
- Rotavirus Infection in Swine: Genotypic Diversity, Immune Responses, and Role of Gut Microbiome in Rotavirus Immunity.Pathogens (Basel, Switzerland) · 2022Review
- Rotavirus Spike Protein VP4 Mediates Viroplasm Assembly by Association to Actin Filaments.Journal of virology · 2022Article
- Review
- Human Virus Genomes Are Enriched in Conserved Adenine/Thymine/Uracil Multiple Tracts That Pause Polymerase Progression.Frontiers in microbiology · 2022Article
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
- Article
- Actin-Dependent Nonlytic Rotavirus Exit and Infectious Virus Morphogenetic Pathway in Nonpolarized Cells.Journal of virology · 2018Article
- Design and Construction of Chimeric VP8-S2 Antigen for Bovine Rotavirus and Bovine Coronavirus.Advanced pharmaceutical bulletin · 2016Article
- Rotavirus infection of cells in culture induces activation of RhoA and changes in the actin and tubulin cytoskeleton.PloS one · 2012Article
- Rotavirus infection activates the UPR but modulates its activity.Virology journal · 2011Article
- Rotavirus NSP4: Cell type-dependent transport kinetics to the exofacial plasma membrane and release from intact infected cells.Virology journal · 2011Article
- Rotaviruses associate with cellular lipid droplet components to replicate in viroplasms, and compounds disrupting or blocking lipid droplets inhibit viroplasm formation and viral replication.Journal of virology · 2010Article
- Sequestration of free tubulin molecules by the viral protein NSP2 induces microtubule depolymerization during rotavirus infection.Journal of virology · 2010Article
- Rotavirus-like particles: a novel nanocarrier for the gut.Journal of biomedicine & biotechnology · 2010Article
- Initiation of hepatitis C virus infection requires the dynamic microtubule network: role of the viral nucleocapsid protein.The Journal of biological chemistry · 2009Article
- Heterogeneity of Raft-type membrane microdomains associated with VP4, the rotavirus spike protein, in Caco-2 and MA 104 cells.Journal of virology · 2007Article
- Hsp70 negatively controls rotavirus protein bioavailability in caco-2 cells infected by the rotavirus RF strain.Journal of virology · 2007Article
- Assembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.Journal of virology · 2006Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
VP4 is an unglycosylated protein of the outer layer of the capsid of rotavirus. It forms spikes that project from the outer layer of mature virions, which is mainly constituted by glycoprotein VP7. VP4 has been implicated in several important functions, such as cell attachment, penetration, hemagglutination, neutralization, virulence, and host range. Previous studies indicated that VP4 is located in the space between the periphery of the viroplasm and the outside of the endoplasmic reticulum in rotavirus-infected cells. Confocal microscopy of infected MA104 monolayers, immunostained with specific monoclonal antibodies, revealed that a significant fraction of VP4 was present at the plasma membrane early after infection. Another fraction of VP4 is cytoplasmic and colocalizes with beta-tubulin. Flow cytometry analysis confirmed that at the early stage of viral infection, VP4 was present on the plasma membrane and that its N-terminal region, the VP8* subunit, was accessible to antibodies. Biotin labeling of the infected cell surface monolayer with a cell-impermeable reagent allowed the identification of the noncleaved form of VP4 that was associated with the glycoprotein VP7. The localization of VP4 was not modified in cells transfected with a plasmid allowing the expression of a fusion protein consisting of VP4 and the green fluorescent protein. The present data suggest that VP4 reaches the plasma membrane through the microtubule network and that other viral proteins are dispensable for its targeting and transport.
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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.