ArticleJournal of virology1998
The molecular chaperone calnexin interacts with the NSP4 enterotoxin of rotavirus in vivo and in vitro.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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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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
22 citing papers in PubMed, 42 citations in OpenAlex.
- N-Glycosylation of Rotavirus NSP4 Protein Affects Viral Replication and Pathogenesis.Journal of virology · 2023Article
- Treading a HOSTile path: Mapping the dynamic landscape of host cell-rotavirus interactions to explore novel host-directed curative dimensions.Virulence · 2021Review
- Perturbation of Wound Healing, Cytoskeletal Organization and Cellular Protein Networks during Hazara Virus Infection.Frontiers in cell and developmental biology · 2017Article
- Rotavirus and Serotonin Cross-Talk in Diarrhoea.PloS one · 2016Article
- Review
- The roles of direct recognition by animal lectins in antiviral immunity and viral pathogenesis.Molecules (Basel, Switzerland) · 2015Review
- Article
- Rotavirus non-structural proteins: structure and function.Current opinion in virology · 2012Review
- 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
- Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Endoplasmic reticulum chaperones are involved in the morphogenesis of rotavirus infectious particles.Journal of virology · 2008Article
- Role of interferon regulatory factor 3 in type I interferon responses in rotavirus-infected dendritic cells and fibroblasts.Journal of virology · 2007Article
- 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
- Spike protein VP4 assembly with maturing rotavirus requires a postendoplasmic reticulum event in polarized caco-2 cells.Journal of virology · 2004Article
- Rotavirus enterotoxin NSP4 binds to the extracellular matrix proteins laminin-beta3 and fibronectin.Journal of virology · 2004Article
- Interaction(s) of rotavirus non-structural protein 4 (NSP4) C-terminal peptides with model membranes.The Biochemical journal · 2004Article
- Antiviral effect of N-butyldeoxynojirimycin against bovine viral diarrhea virus correlates with misfolding of E2 envelope proteins and impairment of their association into E1-E2 heterodimers.Journal of virology · 2001Article
- A functional NSP4 enterotoxin peptide secreted from rotavirus-infected cells.Journal of virology · 2000Article
- ATP is required for correct folding and disulfide bond formation of rotavirus VP7.Journal of virology · 2000Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Calnexin is an endoplasmic reticulum (ER)-associated molecular chaperone proposed to promote folding and assembly of glycoproteins that traverse the secretory pathway in eukaryotic cells. In this study we examined if calnexin interacts with the ER-associated luminal (VP7) and transmembrane (NSP4) proteins of rotavirus. Only glycosylated NSP4 interacted with calnexin and did so in a time-dependent manner (half-life, 20 min). In vitro translation experiments programmed with gene 10 of rhesus rotavirus confirmed that calnexin recognizes only glycosylated NSP4. Castanospermine (a glucosidase I and II inhibitor) experiments established that calnexin associates only with partly deglucosylated (di- or monoglucosylated) NSP4. Furthermore, enzymatic removal of the remaining glucose residues on the N-linked glycan units was essential to disengage the NSP4-calnexin complex. Novel experiments with castanospermine revealed that glucose trimming and the calnexin-NSP4 interaction were not critical for the assembly of infectious virus.
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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.