ArticleNature communications2025
Molecular basis of host recognition of human coronavirus 229E.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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
8 citing papers in PubMed.
- Structure and receptor recognition of type-II feline infectious peritonitis virus spike glycoprotein.The EMBO journal · 2026Article
- Mass Photometry Reveals Distinct ACE2 Binding Stoichiometries across SARS-CoV-2 Omicron Subvariants.The journal of physical chemistry. B · 2026Article
- Mutations to the HCoV-229E spike have counterbalancing effects on serum antibody neutralization and receptor binding.bioRxiv : the preprint server for biology · 2026Article
- Endosomal maturation leads to nucleocapsid conformation change in seasonal coronaviruses.Nagoya journal of medical science · 2026Article
- A neutralizing human antibody induces movement of the HCoV-229E receptor binding domain.Communications biology · 2025Article
- The Dual Role of A20 (TNFAIP3) in Viral Infection: A Context-Dependent Regulator of Immunity and Pathogenesis.Viruses · 2025Review
- Review
- From zoonotic spillover to endemicity: the broad determinants of human coronavirus tropism.mBio · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Human coronavirus 229E (HCoV-229E) is the earliest CoV found to infect humans. It binds to the human aminopeptidase N (hAPN) through the receptor binding domain (RBD) of its spike (S) protein to achieve host recognition. We present the cryo-electron microscopy structure of two HCoV-229E S protein in complex with a dimeric hAPN to provide structural insights on how the HCoV-229E S protein opens up its RBD to engage with its host receptor, information that is currently missing among alphacoronaviruses to which HCoV-229E belong. We quantitatively profile the glycosylation of HCoV-229E S protein and hAPN to deduce the glyco-shielding effects pertinent to antigenicity and host recognition. Finally, we present an atomic model of fully glycosylated HCoV-229E S in complex with hAPN anchored on their respective membrane bilayers to recapitulate the structural basis of the first step of host infection by HCoV-229E.
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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.