ArticleThe Journal of biological chemistry2011
Determinants of the specificity of rotavirus interactions with the alpha2beta1 integrin.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 29 citations in OpenAlex.
- Platelets in infection: intrinsic roles and functional outcomes.Frontiers in immunology · 2025Review
- Of vascular defense, hemostasis, cancer, and platelet biology: an evolutionary perspective.Cancer metastasis reviews · 2022Review
- Platelets in Viral Infections - Brave Soldiers or Trojan Horses.Frontiers in immunology · 2022Review
- Article
- A Champion of Host Defense: A Generic Large-Scale Cause for Platelet Dysfunction and Depletion in Infection.Seminars in thrombosis and hemostasis · 2020Review
- An Effective Platform for Exploring Rotavirus Receptors by Bacterial Surface Display System.Virologica Sinica · 2020Article
- Evidence for Viral Induction of Biliary Atresia: A Review.Journal of clinical and translational hepatology · 2018Review
- Enteric Species F Human Adenoviruses use Laminin-Binding Integrins as Co-Receptors for Infection of Ht-29 Cells.Scientific reports · 2018Article
- Human blood platelets and viruses: defense mechanism and role in the removal of viral pathogens.Thrombosis journal · 2018Review
- Experimental Adaptation of Rotaviruses to Tumor Cell Lines.PloS one · 2016Article
- The role of platelets in the pathogenesis of viral hemorrhagic fevers.PLoS neglected tropical diseases · 2014Review
- Relative roles of GM1 ganglioside, N-acylneuraminic acids, and α2β1 integrin in mediating rotavirus infection.Journal of virology · 2014Article
- The spike protein VP4 defines the endocytic pathway used by rotavirus to enter MA104 cells.Journal of virology · 2013Article
- Enhancing integrin α1 inserted (I) domain affinity to ligand potentiates integrin α1β1-mediated down-regulation of collagen synthesis.The Journal of biological chemistry · 2012Article
- Rotavirus and biliary atresia: can causation be proven?Current opinion in gastroenterology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The human α2β1 integrin binds collagen and acts as a cellular receptor for rotaviruses and human echovirus 1. These ligands require the inserted (I) domain within the α2 subunit of α2β1 for binding. Previous studies have identified the binding sites for collagen and echovirus 1 in the α2 I domain. We used CHO cells expressing mutated α2β1 to identify amino acids involved in binding to human and animal rotaviruses. Residues where mutation affected rotavirus binding were located in several exposed loops and adjacent regions of the α2 I domain. Binding by all rotaviruses was eliminated by mutations in the activation-responsive αC-α6 and αF helices. This is a novel feature that distinguishes rotavirus from other α2β1 ligands. Mutation of residues that co-ordinate the metal ion (Ser-153, Thr-221, and Glu-256 in α2 and Asp-130 in β1) and nearby amino acids (Ser-154, Gln-215, and Asp-219) also inhibited rotavirus binding. The importance of most of these residues was greatest for binding by human rotaviruses. These mutations inhibit collagen binding to α2β1 (apart from Glu-256) but do not affect echovirus binding. Overall, residues where mutation affected both rotavirus and collagen recognition are located at one side of the metal ion-dependent adhesion site, whereas those important for collagen alone cluster nearby. Mutations eliminating rotavirus and echovirus binding are distinct, consistent with the respective preference of these viruses for activated or inactive α2β1. In contrast, rotavirus and collagen utilize activated α2β1 and show an overlap in α2β1 residues important for binding.
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What OpenQuestion holds
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.