ArticleJournal of virology2006
Rotavirus nonstructural glycoprotein NSP4 is secreted from the apical surfaces of polarized epithelial cells.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 55 citations in OpenAlex.
- Review
- A novel glycoform of the rotavirus outer capsid protein VP7 is secreted from polarized cells and activates innate immune cells.Journal of virology · 2026Article
- Comparative Genomics of Viral Genomes and Identification of Three Novel Viroporin-Like Superfamilies.Microbial physiology · 2026Article
- The leader of the capsid protein fromJournal of virology · 2025Article
- Review
- Understanding the penetrance of intrinsic protein disorder in rotavirus proteome.International journal of biological macromolecules · 2020Article
- Porcine rotavirus mainly infects primary porcine enterocytes at the basolateral surface.Veterinary research · 2019Article
- Immunomodulating dose of levamisole stimulates innate immune response and prevents intestinal damage in porcine rotavirus diarrhea: a restricted-randomized, single-blinded, and placebo-controlled clinical trial.Tropical animal health and production · 2019Article
- Rotavirus NSP4Virus genes · 2017Article
- Intradermal delivery of DNA encoding HCV NS3 and perforin elicits robust cell-mediated immunity in mice and pigs.Gene therapy · 2016Article
- Pathophysiological Consequences of Calcium-Conducting Viroporins.Annual review of virology · 2015Review
- Article
- Increase in DNA vaccine efficacy by virosome delivery and co-expression of a cytolytic protein.Clinical & translational immunology · 2014Article
- Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1.Virology journal · 2013Article
- Rotavirus NSP4 Triggers Secretion of Proinflammatory Cytokines from Macrophages via Toll-Like Receptor 2.Journal of virology · 2013Article
- Genetic divergence of rotavirus nonstructural protein 4 results in distinct serogroup-specific viroporin activity and intracellular punctate structure morphologies.Journal of virology · 2012Article
- Rotavirus infection of cells in culture induces activation of RhoA and changes in the actin and tubulin cytoskeleton.PloS one · 2012Article
- Elucidation of the Rotavirus NSP4-Caveolin-1 and -Cholesterol Interactions Using Synthetic Peptides.Journal of amino acids · 2012Article
- Rotavirus NSP4 is secreted from infected cells as an oligomeric lipoprotein and binds to glycosaminoglycans on the surface of non-infected cells.Virology journal · 2011Article
- Novel pentameric structure of the diarrhea-inducing region of the rotavirus enterotoxigenic protein NSP4.Journal of virology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NSP4, a nonstructural glycoprotein encoded by rotavirus, is involved in the morphogenesis of virus particles in the endoplasmic reticulum of infected cells. NSP4 is also implicated in the pathophysiology of rotavirus-induced diarrhea by acting as an enterotoxin. To mediate enterotoxic effects in vivo, NSP4 must be secreted or released from rotavirus-infected cells in a soluble form; however, previous studies have indicated that NSP4 is a transmembrane glycoprotein localized within endomembrane compartments in infected cells. In this study, we examined the fate of NSP4 synthesized in Caco-2 cells infected with bovine rotavirus. Our studies reveal that NSP4 is actively secreted into the culture medium, preferentially from the infected-cell apical surface. The secretion of NSP4 is dramatically inhibited by brefeldin A and monensin, suggesting that a Golgi-dependent pathway is involved in release of the protein. In agreement with the proposed involvement of the Golgi apparatus during secretion, secreted NSP4 appears to undergo additional posttranslational modification compared to its cell-associated counterpart and is partially resistant to deglycosylation by endoglycosidase H. Our experiments identify a novel, soluble form of NSP4 secreted from virus-infected cells with the potential to carry out the enterotoxigenic role previously attributed to recombinant forms of the protein.
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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.