ArticleNature communications2017
Crystal structure of the receptor binding domain of the spike glycoprotein of human betacoronavirus HKU1.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53 citing papers in PubMed.
- Temperature-dependent replication and sensitivity to innate immunity of human coronavirus HKU1.Nature communications · 2026Article
- Epidemiological characteristics of human coronaviruses among populations with acute respiratory infections: surveillance data from jing'an district, Shanghai, 2024-2025.Preventive medicine reports · 2026Article
- Review
- A novel chimeric coronavirus spike vaccine combining SARS-CoV-2 RBD and scaffold domains from HKU-1 elicits potent neutralising antibody responses.NPJ vaccines · 2025Article
- Human coronavirus HKU1 neutralization by glycan receptor mimicry.bioRxiv : the preprint server for biology · 2025Article
- Dipeptidase 1 is a functional receptor for a porcine coronavirus.Nature microbiology · 2025Article
- Five-Year (2017-2022) Evolutionary Dynamics of Human Coronavirus HKU1 in Southern France With Emergence of Viruses Harboring Spike H512R Substitution.Journal of medical virology · 2025Article
- Identification of the critical residues of TMPRSS2 for entry and host range of human coronavirus HKU1.Journal of virology · 2024Article
- Article
- Positive selection, genetic recombination, and intra-host evolution in novel equine coronavirus genomes and other members of theMicrobiology spectrum · 2024Article
- Structural basis for the interaction between human coronavirus HKU1 spike receptor binding domain and its receptor TMPRSS2.Cell discovery · 2024Article
- Article
- Structural basis for the recognition of HCoV-HKU1 by human TMPRSS2.Cell research · 2024Article
- Human coronavirus OC43 nanobody neutralizes virus and protects mice from infection.Journal of virology · 2024Article
- ACE2-using merbecoviruses: Further evidence of convergent evolution of ACE2 recognition by NeoCoV and other MERS-CoV related viruses.Cell insight · 2024Review
- Human coronavirus HKU1 recognition of the TMPRSS2 host receptor.bioRxiv : the preprint server for biology · 2024Article
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- Cryo-EM reveals binding of linoleic acid to SARS-CoV-2 spike glycoprotein, suggesting an antiviral treatment strategy.Acta crystallographica. Section D, Structural biology · 2023Article
- Article
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9 authors.
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Abstract
Human coronavirus (CoV) HKU1 is a pathogen causing acute respiratory illnesses and so far little is known about its biology. HKU1 virus uses its S1 subunit C-terminal domain (CTD) and not the N-terminal domain like other lineage A β-CoVs to bind to its yet unknown human receptor. Here we present the crystal structure of HKU1 CTD at 1.9 Å resolution. The structure consists of three subdomains: core, insertion and subdomain-1 (SD-1). While the structure of the core and SD-1 subdomains of HKU1 are highly similar to those of other β-CoVs, the insertion subdomain adopts a novel fold, which is largely invisible in the cryo-EM structure of the HKU1 S trimer. We identify five residues in the insertion subdomain that are critical for binding of neutralizing antibodies and two residues essential for receptor binding. Our study contributes to a better understanding of entry, immunity and evolution of CoV S proteins.
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