ArticleeLife2019
The human coronavirus HCoV-229E S-protein structure and receptor binding.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
149 citing papers in PubMed.
- Integrated multi-PTM omics reveals key host pathways in human coronavirus 229E infection.Redox biology · 2026Article
- Addressing the zoonotic threat of merbecoviruses.Nature microbiology · 2026Review
- OC43 clinical isolate spike proteins have distinct carbohydrate-binding properties.Nature communications · 2026Article
- Article
- FUT8-mediated core fucosylation of receptor APN drives entry of multiple alphacoronaviruses.PLoS pathogens · 2026Article
- Cetacean coronavirus spikes highlight S glycoprotein structural plasticity.PLoS pathogens · 2026Article
- Knockout of aminopeptidase N3 confers resistance to low concentrations of Bacillus thuringiensis Cry4Ba protoxin in Aedes aegypti.Parasites & vectors · 2026Article
- SARS-CoV-2 fusion-peptide-directed antibodies are elicited by natural infection and can mediate broad sarbecovirus neutralization.Cell reports · 2026Article
- Mutations to the HCoV-229E spike have counterbalancing effects on serum antibody neutralization and receptor binding.bioRxiv : the preprint server for biology · 2026Article
- Human alphacoronavirus replication and innate immune induction in airway culture systems.mBio · 2026Article
- A neutralizing human antibody induces movement of the HCoV-229E receptor binding domain.Communications biology · 2025Article
- Review
- An integrated workflow for structural virology with a 100 keV electron microscope.bioRxiv : the preprint server for biology · 2025Article
- Receptor affinity-selective differential dynamics of membrane fusion initiation govern deltacoronavirus cross-species transmission.Science China. Life sciences · 2025Article
- Current Status and Challenges of Vaccine Development for Seasonal Human Coronaviruses.Vaccines · 2025Review
- From zoonotic spillover to endemicity: the broad determinants of human coronavirus tropism.mBio · 2025Review
- A novel linear B-cell epitope on S2 protein of transmissible gastroenteritis virus identified using a monoclonal antibody.BMC veterinary research · 2025Article
- Inhibition of Human Coronavirus 229E by Lactoferrin-Derived Peptidomimetics.Pharmaceutics · 2025Article
- Review
- Dual-Locking the SARS-CoV-2 Spike Trimer: An Amphipathic Molecular "Bolt" Stabilizes Conserved Druggable Interfaces for Coronavirus Inhibition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
89 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
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The coronavirus S-protein mediates receptor binding and fusion of the viral and host cell membranes. In HCoV-229E, its receptor binding domain (RBD) shows extensive sequence variation but how S-protein function is maintained is not understood. Reported are the X-ray crystal structures of Class III-V RBDs in complex with human aminopeptidase N (hAPN), as well as the electron cryomicroscopy structure of the 229E S-protein. The structures show that common core interactions define the specificity for hAPN and that the peripheral RBD sequence variation is accommodated by loop plasticity. The results provide insight into immune evasion and the cross-species transmission of 229E and related coronaviruses. We also find that the 229E S-protein can expose a portion of its helical core to solvent. This is undoubtedly facilitated by hydrophilic subunit interfaces that we show are conserved among coronaviruses. These interfaces likely play a role in the S-protein conformational changes associated with membrane fusion.
Indexed as
Identifiers
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.