ArticleJournal of virology2004
Spike protein VP4 assembly with maturing rotavirus requires a postendoplasmic reticulum event in polarized caco-2 cells.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Treading a HOSTile path: Mapping the dynamic landscape of host cell-rotavirus interactions to explore novel host-directed curative dimensions.Virulence · 2021Review
- Recent advances in rotavirus reverse genetics and its utilization in basic research and vaccine development.Archives of virology · 2021Review
- Actin-Dependent Nonlytic Rotavirus Exit and Infectious Virus Morphogenetic Pathway in Nonpolarized Cells.Journal of virology · 2018Article
- Inflammatory and oxidative stress in rotavirus infection.World journal of virology · 2016Review
- Evidences and consequences of extra-intestinal spread of rotaviruses in humans and animals.Virusdisease · 2014Article
- Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.Journal of virology · 2011Article
- Function of membrane rafts in viral lifecycles and host cellular response.Biochemistry research international · 2011Article
- Rotavirus antagonism of the innate immune response.Viruses · 2009Article
- Bluetongue virus outer capsid protein VP5 interacts with membrane lipid rafts via a SNARE domain.Journal of virology · 2008Article
- Role for actin in the polarized release of rotavirus.Journal of virology · 2007Article
- Heterogeneity of Raft-type membrane microdomains associated with VP4, the rotavirus spike protein, in Caco-2 and MA 104 cells.Journal of virology · 2007Article
- Rotavirus nonstructural glycoprotein NSP4 is secreted from the apical surfaces of polarized epithelial cells.Journal of virology · 2006Article
- Assembly of highly infectious rotavirus particles recoated with recombinant outer capsid proteins.Journal of virology · 2006Article
- Rotavirus spike protein VP4 binds to and remodels actin bundles of the epithelial brush border into actin bodies.Journal of virology · 2006Article
- Dissecting rotavirus particle-raft interaction with small interfering RNAs: insights into rotavirus transit through the secretory pathway.Journal of virology · 2006Article
- N- and C-terminal cooperation in rotavirus enterotoxin: novel mechanism of modulation of the properties of a multifunctional protein by a structurally and functionally overlapping conformational domain.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
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotavirus assembly is a multistep process that requires the successive association of four major structural proteins in three concentric layers. It has been assumed until now that VP4, the most external viral protein that forms the spikes of mature virions, associates with double-layer particles within the endoplasmic reticulum (ER) in conjunction with VP7 and with the help of a nonstructural protein, NSP4. VP7 and NSP4 are two glycosylated proteins. However, we recently described a strong association of VP4 with raft-type membrane microdomains, a result that makes the ER a highly questionable site for the final assembly of rotavirus, since rafts are thought to be absent from this compartment. In this study, we used tunicamycin (TM), a drug known to block the first step of protein N glycosylation, as a tool to dissect rotavirus assembly. We show that, as expected, TM blocks viral protein glycosylation and also decreases virus infectivity. In the meantime, viral particles were blocked as enveloped particles in the ER. Interestingly, TM does not prevent the targeting of VP4 to the cell surface nor its association with raft membranes, whereas the infectivity associated with the raft fractions strongly decreased. VP4 does not colocalize with the ER marker protein disulfide-isomerase even when viral particles were blocked by TM in this compartment. These results strongly support a primary role for raft membranes in rotavirus final assembly and the fact that VP4 assembly with the rest of the particle is an extrareticular event.
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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.