ArticleJournal of virology2004
Rotavirus enterotoxin NSP4 binds to the extracellular matrix proteins laminin-beta3 and fibronectin.
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 25 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 50 citations in OpenAlex.
- Acute kidney injury and hyponatremia in hospitalized patients with rotavirus infection.PloS one · 2026Article
- Rotavirus Infections: Pathophysiology, Symptoms, and Vaccination.Pathogens (Basel, Switzerland) · 2025Review
- Prospects for the use of viral proteins for the construction of chimeric toxins.Archives of virology · 2024Review
- Host Subcellular Organelles: Targets of Viral Manipulation.International journal of molecular sciences · 2024Review
- Rotavirus infection-associated central nervous system complications: clinicoradiological features and potential mechanisms.Clinical and experimental pediatrics · 2022Article
- Rotavirus infection.Nature reviews. Disease primers · 2017Review
- Rotavirus NSP4Virus genes · 2017Article
- Review
- Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1.Virology journal · 2013Article
- Rotavirus non-structural proteins: structure and function.Current opinion in virology · 2012Review
- Diverse microbial interactions with the basement membrane barrier.Trends in microbiology · 2012Review
- Pathogenic Naegleria fowleri and non-pathogenic Naegleria lovaniensis exhibit differential adhesion to, and invasion of, extracellular matrix proteins.Microbiology (Reading, England) · 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
- Rotavirus NSP4: Cell type-dependent transport kinetics to the exofacial plasma membrane and release from intact infected cells.Virology journal · 2011Article
- Conformational Differences Unfold a Wide Range of Enterotoxigenic Abilities Exhibited by rNSP4 Peptides from Different Rotavirus Strains.The open virology journal · 2011Article
- Infectious diarrhea: Cellular and molecular mechanisms.Gut microbes · 2010Article
- Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Laminin isoforms in development and disease.Journal of molecular medicine (Berlin, Germany) · 2007Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotavirus is the most important cause of viral gastroenteritis and dehydrating diarrhea in young children. Rotavirus nonstructural protein 4 (NSP4) is an enterotoxin that was identified as an important agent in symptomatic rotavirus infection. To identify cellular proteins that interact with NSP4, a two-hybrid technique with Saccharomyces cerevisiae was used. NSP4 cDNA, derived from the human rotavirus strain Wa, was cloned into the yeast shuttle vector pGBKT7. An intestinal cDNA library derived from Caco-2 cells cloned into the yeast shuttle vector pGAD10 was screened for proteins that interact with NSP4. Protein interactions were confirmed in vivo by coimmunoprecipitation and immunohistochemical colocalization. After two-hybrid library screening, we repeatedly isolated cDNAs encoding the extracellular matrix (ECM) protein laminin-beta3 (amino acids [aa] 274 to 878) and a cDNA encoding the ECM protein fibronectin (aa 1755 to 1884). Using deletion mutants of NSP4, we mapped the region of interaction with the ECM proteins between aa 87 and 145. Deletion analysis of laminin-beta3 indicated that the region comprising aa 726 to 875 of laminin-beta3 interacts with NSP4. Interaction of NSP4 with either laminin-beta3 or fibronectin was confirmed by coimmunoprecipitation. NSP4 was present in infected enterocytes and in the basement membrane (BM) of infected neonatal mice and colocalized with laminin-beta3, indicating a physiological interaction. In conclusion, two-hybrid screening with NSP4 yielded two potential target proteins, laminin-beta3 and fibronectin, interacting with the enterotoxin NSP4. The release of NSP4 from the basal side of infected epithelial cells and the subsequent binding to ECM proteins localized at the BM may signify a new mechanism by which rotavirus disease is established.
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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.