ArticleJournal of virology2003
Interactions of rotavirus VP4 spike protein with the endosomal protein Rab5 and the prenylated Rab acceptor PRA1.
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 16 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.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Vaccine evaluation and genotype characterization in children infected with rotavirus in Qatar.Pediatric research · 2023Article
- Rotavirus Spike Protein VP4 Mediates Viroplasm Assembly by Association to Actin Filaments.Journal of virology · 2022Article
- Genetic Diversity of Human Rotavirus A Among Hospitalized Children Under-5 Years in Lebanon.Frontiers in immunology · 2020Article
- The C Terminus of Rotavirus VP4 Protein Contains an Actin Binding Domain Which Requires Cooperation with the Coiled-Coil Domain for Actin Remodeling.Journal of virology · 2019Article
- Actin-Dependent Nonlytic Rotavirus Exit and Infectious Virus Morphogenetic Pathway in Nonpolarized Cells.Journal of virology · 2018Article
- Viral interactions with host cell Rab GTPases.Small GTPases · 2018Review
- A role for prenylated rab acceptor 1 in vertebrate photoreceptor development.BMC neuroscience · 2012Article
- HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation.Journal of molecular biology · 2011Review
- Rhesus rotavirus entry into a polarized epithelium is endocytosis dependent and involves sequential VP4 conformational changes.Journal of virology · 2011Article
- Proteome-wide dysregulation by PRA1 depletion delineates a role of PRA1 in lipid transport and cell migration.Molecular & cellular proteomics : MCP · 2011Article
- Silencing of the rotavirus NSP4 protein decreases the incidence of biliary atresia in murine model.PloS one · 2011Article
- A Rab-GAP TBC domain protein binds hepatitis C virus NS5A and mediates viral replication.Journal of virology · 2007Article
- Rab5 mediates an amyloid precursor protein signaling pathway that leads to apoptosis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- Participation of rab5, an early endosome protein, in hepatitis C virus RNA replication machinery.Journal of virology · 2007Article
- Rotavirus spike protein VP4 binds to and remodels actin bundles of the epithelial brush border into actin bodies.Journal of virology · 2006Article
- Rotavirus assembly: an alternative model that utilizes an atypical trafficking pathway.Current topics in microbiology and immunology · 2006Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotavirus spike protein VP4 is implicated in several important functions, such as cell attachment, penetration, hemagglutination, neutralization, virulence, and host range. It is present at the plasma membrane and colocalizes with the cytoskeleton in infected cells. We looked for cellular partners responsible for the localization of VP4 by two-hybrid screening of a monkey CV1 cell cDNA library. In the screen we isolated repeatedly three cDNAs encoding either two isoforms (a and c) of Rab5 protein or the prenylated Rab acceptor (PRA1). The small GTPase Rab5 is a molecule regulating the vesicular traffic and the motility of early endosomes along microtubules. Rab5 interacts with a large number of effectors, in particular with PRA1. Interactions of VP4 with both partners, Rab5 and PRA1, were confirmed by coimmunoprecipitation from infected- or transfected-cell lysates. Interaction of Rab5 and PRA1 was restricted to free VP4, since neither triple-layered particles nor NSP4-VP4-VP7 heterotrimeric complexes could be coprecipitated. Site-directed and deletion mutants of VP4 were used to map a VP4 domain(s) interacting with Rab5 or PRA1. Of the 10 mutants tested, 2 interacted exclusively with a single partner. In contrast, the domain extending from amino acids 560 to 722 of VP4 is essential for both interactions. These results suggest that Rab5 and PRA1 may be involved in the localization and trafficking of VP4 in infected cells.
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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.