ArticleVirus research2007
Rotavirus NSP4 interacts with both the amino- and carboxyl-termini of caveolin-1.
Article in Virus research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Review
- Caveolae as Potential Hijackable Gates in Cell Communication.Frontiers in cell and developmental biology · 2020Review
- The Dengue Virus Nonstructural Protein 1 (NS1) Is Secreted from Mosquito Cells in Association with the Intracellular Cholesterol Transporter Chaperone Caveolin Complex.Journal of virology · 2019Article
- Secondary Structure Analysis of a Functional Construct of Caveolin-1 Reveals a Long C-Terminal Helix.Biophysical journal · 2015Article
- Mutational analysis of the rotavirus NSP4 enterotoxic domain that binds to caveolin-1.Virology journal · 2013Article
- Mandarin fish caveolin 1 interaction with major capsid protein of infectious spleen and kidney necrosis virus and its role in early stages of infection.Journal of virology · 2013Article
- Elucidation of the Rotavirus NSP4-Caveolin-1 and -Cholesterol Interactions Using Synthetic Peptides.Journal of amino acids · 2012Article
- 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
- New glimpses of caveolin-1 functions in embryonic development and human diseases.Frontiers in biology · 2011Review
- Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A new N-terminal recognition domain in caveolin-1 interacts with sterol carrier protein-2 (SCP-2).Biochemistry · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Rotavirus NSP4 plays multiple roles in viral pathogenesis, morphogenesis and replication. We previously reported a direct interaction between full-length NSP4 and the enterotoxic peptide composed of NSP4 residues 114-135 with full-length caveolin-1, the structural protein of caveolae. Caveolin-1 forms a hairpin loop in the cytoplasmic leaflet of plasma membrane caveolae. This unique orientation results in both termini of caveolin-1 exposed to the cytoplasm. The goal of this study was to map the caveolin-1 residues that interact with NSP4 to obtain a more complete picture of this binding event. Utilizing reverse yeast two-hybrid analyses and direct peptide binding assays, the NSP4 binding site was localized to caveolin-1 residues 2-22 and 161-178, at the amino- and carboxyl-termini, respectively. However, NSP4 binding to one of the termini was sufficient for the interaction.
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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.