ArticleProceedings of the National Academy of Sciences of the United States of America2008
Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 82 citations in OpenAlex.
- Article
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- Prospects for the use of viral proteins for the construction of chimeric toxins.Archives of virology · 2024Review
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- Intercellular Transport of Viral Proteins.Results and problems in cell differentiation · 2024Review
- Engagement of αFrontiers in microbiology · 2024Article
- Single-Cell Transcriptome Atlas of Newcastle Disease Virus in Chickens BothMicrobiology spectrum · 2023Article
- N-Glycosylation of Rotavirus NSP4 Protein Affects Viral Replication and Pathogenesis.Journal of virology · 2023Article
- Calcium-sensing receptor acts as an antiviral factor for rotavirus infections and participates in cellular antiviral response.Iranian journal of basic medical sciences · 2022Article
- Review
- Evolutionary changes between pre- and post-vaccine South African group A G2P[4] rotavirus strains, 2003-2017.Microbial genomics · 2022Article
- EnterotoxigenicPathogens (Basel, Switzerland) · 2022Review
- Rotavirus induces intercellular calcium waves through ADP signaling.Science (New York, N.Y.) · 2020Article
- Rotavirus infection.Nature reviews. Disease primers · 2017Review
- Rotavirus NSP4Virus genes · 2017Article
- Higher Expression Level and Lower Toxicity of Genetically Spliced Rotavirus NSP4 in Comparison to the Full-Length Protein inIranian journal of biotechnology · 2016Article
- Human Intestinal Enteroids: a New Model To Study Human Rotavirus Infection, Host Restriction, and Pathophysiology.Journal of virology · 2016Article
- Use of genetically-encoded calcium indicators for live cell calcium imaging and localization in virus-infected cells.Methods (San Diego, Calif.) · 2015Article
- Beyond RGD: virus interactions with integrins.Archives of virology · 2015Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Rotavirus NSP4 is a viral enterotoxin capable of causing diarrhea in neonatal mice. This process is initiated by the binding of extracellular NSP4 to target molecule(s) on the cell surface that triggers a signaling cascade leading to diarrhea. We now report that the integrins alpha1beta1 and alpha2beta1 are receptors for NSP4. NSP4 specifically binds to the alpha1 and alpha2 I domains with apparent K(d) = 1-2.7 muM. Binding is mediated by the I domain metal ion-dependent adhesion site motif, requires Mg(2+) or Mn(2+), is abolished with EDTA, and an NSP4 point mutant, E(120)A, fails to bind alpha2 integrin I domain. NSP4 has two distinct integrin interaction domains. NSP4 amino acids 114-130 are essential for binding to the I domain, and NSP4 peptide 114-135 blocks binding of the natural ligand, collagen I, to integrin alpha2. NSP4 amino acids 131-140 are not associated with the initial binding to the I domain, but elicit signaling that leads to the spreading of attached C2C12-alpha2 cells, mouse myoblast cells stably expressing the human alpha2 integrin. NSP4 colocalizes with integrin alpha2 on the basolateral surface of rotavirus-infected polarized intestinal epithelial (Caco-2) cells as well as surrounding noninfected cells. NSP4 mutants that fail to bind or signal through integrin alpha2 were attenuated in diarrhea induction in neonatal mice. These results indicate that NSP4 interaction with integrin alpha1 and alpha2 is an important component of enterotoxin function and rotavirus pathogenesis, further distinguishing this viral virulence factor from other microbial enterotoxins.
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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.