ArticleJournal of virology2012
Structural basis of rotavirus strain preference toward N-acetyl- or N-glycolylneuraminic acid-containing receptors.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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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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Who cites it
25 citing papers in PubMed, 46 citations in OpenAlex.
- Specific binding of human P[28] rotavirus VP8* protein to blood group ABH antigens on type 1 chains.PLoS pathogens · 2025Article
- Virus-Glycan Interactions Studied by Solute NMR.Methods in molecular biology (Clifton, N.J.) · 2025Article
- The forecasting power of the mucin-microbiome interplay in livestock respiratory diseases.The veterinary quarterly · 2024Article
- Benzene with Alkyl Chains Is a Universal Scaffold for Multivalent Virucidal Antivirals.ACS central science · 2024Article
- An In Silico Functional Analysis of Non-Synonymous Single-Nucleotide Polymorphisms of BovinePathogens (Basel, Switzerland) · 2023Article
- Involvement of sialoglycans in SARS-COV-2 infection: Opportunities and challenges for glyco-based inhibitors.IUBMB life · 2022Review
- Wild and domestic animals variably display Neu5Ac and Neu5Gc sialic acids.Glycobiology · 2022Article
- Structural Basis of Glycan Recognition of Rotavirus.Frontiers in molecular biosciences · 2021Review
- The Basis of Peracetic Acid Inactivation Mechanisms for Rotavirus and Tulane Virus under Conditions Relevant for Vegetable Sanitation.Applied and environmental microbiology · 2020Article
- Human Neonatal Rotavirus Vaccine (RV3-BB) Produces Vaccine Take Irrespective of Histo-Blood Group Antigen Status.The Journal of infectious diseases · 2020Article
- Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Structures of MERS-CoV spike glycoprotein in complex with sialoside attachment receptors.Nature structural & molecular biology · 2019Article
- Glycan recognition in globally dominant human rotaviruses.Nature communications · 2018Article
- The Sodium Sialic Acid Symporter FromFrontiers in chemistry · 2018Article
- Effects of Sialic Acid Modifications on Virus Binding and Infection.Trends in microbiology · 2016Review
- Diversity in Rotavirus-Host Glycan Interactions: A "Sweet" Spectrum.Cellular and molecular gastroenterology and hepatology · 2016Review
- Human milk contains novel glycans that are potential decoy receptors for neonatal rotaviruses.Molecular & cellular proteomics : MCP · 2014Article
- The sweet spot: defining virus-sialic acid interactions.Nature reviews. Microbiology · 2014Review
- Carbohydrate recognition by rotaviruses.Journal of structural and functional genomics · 2014Review
- Rules and exceptions: sialic acid variants and their role in determining viral tropism.Journal of virology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rotavirus spike protein domain VP8* is essential for recognition of cell surface carbohydrate receptors, notably those incorporating N-acylneuraminic acids (members of the sialic acid family). N-Acetylneuraminic acids occur naturally in both animals and humans, whereas N-glycolylneuraminic acids are acquired only through dietary uptake in normal human tissues. The preference of animal rotaviruses for these natural N-acylneuraminic acids has not been comprehensively established, and detailed structural information regarding the interactions of different rotaviruses with N-glycolylneuraminic acids is lacking. In this study, distinct specificities of VP8* for N-acetyl- and N-glycolylneuraminic acids were revealed using biophysical techniques. VP8* protein from the porcine rotavirus CRW-8 and the bovine rotavirus Nebraska calf diarrhea virus (NCDV) showed a preference for N-glycolyl- over N-acetylneuraminic acids, in contrast to results obtained with rhesus rotavirus (RRV). Crystallographic structures of VP8* from CRW-8 and RRV with bound methyl-N-glycolylneuraminide revealed the atomic details of their interactions. We examined the influence of amino acid type at position 157, which is proximal to the ligand's N-acetyl or N-glycolyl moiety and can mutate upon cell culture adaptation. A structure-based hypothesis derived from these results could account for rotavirus discrimination between the N-acylneuraminic acid forms. Infectivity blockade experiments demonstrated that the determined carbohydrate specificities of these VP8* domains directly correlate with those of the corresponding infectious virus. This includes an association between CRW-8 adaption to cell culture, decreased competition by N-glycolylneuraminic acid for CRW-8 infectivity, and a Pro157-to-Ser157 mutation in VP8* that reduces binding affinity for N-glycolylneuraminic acid.
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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.