ArticleNature structural & molecular biology2019
Structural basis for human coronavirus attachment to sialic acid receptors.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 386 papers, 4 of them syntheses that pooled it.
What it found
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The trial behind it
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
386 citing papers in PubMed, 4 syntheses or guidelines pooled it, 634 citations in OpenAlex.
- Pooled it
- COVID-19 in comorbid chronic diseased patients, pregnant and lactating women: pathophysiology, available drug treatment, and the most suitable protocol regimen in each group.Inflammopharmacology · 2025Pooled it
- A pooled analysis of the incidence and mortality risk of atrial fibrillation in patients with COVID-19.PeerJ · 2024Pooled it
- Drug repositioning: Progress and challenges in drug discovery for various diseases.European journal of medicinal chemistry · 2022Pooled it
- Targeting virus-glycan recognition in influenza viruses and coronaviruses: from the molecular principles to glycomimetic antivirals strategies.RSC chemical biology · 2026Review
- Structural dynamics and allosteric communication of a SARS-like bat coronavirus spike glycoprotein.Biophysical journal · 2026Article
- Structure and receptor recognition of type-II feline infectious peritonitis virus spike glycoprotein.The EMBO journal · 2026Article
- Sialic acids are a barrier to the entry of non-influenza orthomyxoviruses.PLoS pathogens · 2026Article
- Article
- Exploring coronavirus cell entry with functional viromics.Journal of virology · 2026Review
- OC43 clinical isolate spike proteins have distinct carbohydrate-binding properties.Nature communications · 2026Article
- Enhanced sialic acid engagement at physiological temperatures by reovirus σ1 mutants facilitates infection of breast cancer cells with low levels of high-affinity receptors.Journal of virology · 2026Article
- Molecular Surveillance of Coronaviruses in Riyadh (2025-2026): Persistent Genotype C and Conserved N-Glycosylation Motifs in Human Coronavirus OC43.International journal of molecular sciences · 2026Article
- FUT1- and GAL3ST2-mediated cellular glycan remodeling broadly restricts sialic acid-dependent viral infections.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Pandemic-driven immune imprinting accelerates evolution of human coronavirus OC43.PLoS neglected tropical diseases · 2026Article
- AI-guided prefusion stabilization of the human coronavirus OC43 spike protein enables universal embecovirus antigen design.PLoS pathogens · 2026Article
- Host Glycan-Lectin Interplay in SARS-CoV-2 Infection.International journal of molecular sciences · 2026Review
- Whole-Genome Characterization of Rodent Coronaviruses (RCoVs) in Thailand, 2024-2025.Transboundary and emerging diseases · 2026Article
- An integrated workflow for structural virology with a 100 keV electron microscope.bioRxiv : the preprint server for biology · 2025Article
- From zoonotic spillover to endemicity: the broad determinants of human coronavirus tropism.mBio · 2025Review
326 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Coronaviruses cause respiratory tract infections in humans and outbreaks of deadly pneumonia worldwide. Infections are initiated by the transmembrane spike (S) glycoprotein, which binds to host receptors and fuses the viral and cellular membranes. To understand the molecular basis of coronavirus attachment to oligosaccharide receptors, we determined cryo-EM structures of coronavirus OC43 S glycoprotein trimer in isolation and in complex with a 9-O-acetylated sialic acid. We show that the ligand binds with fast kinetics to a surface-exposed groove and that interactions at the identified site are essential for S-mediated viral entry into host cells, but free monosaccharide does not trigger fusogenic conformational changes. The receptor-interacting site is conserved in all coronavirus S glycoproteins that engage 9-O-acetyl-sialogycans, with an architecture similar to those of the ligand-binding pockets of coronavirus hemagglutinin esterases and influenza virus C/D hemagglutinin-esterase fusion glycoproteins. Our results demonstrate these viruses evolved similar strategies to engage sialoglycans at the surface of target cells.
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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.