ArticleActa crystallographica. Section D, Structural biology2018
Crystal structure of the post-fusion core of the Human coronavirus 229E spike protein at 1.86 Å resolution.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.
- The Spike of SARS-CoV-2: Uniqueness and Applications.Frontiers in immunology · 2021Pooled it
- CGM23 corresponds to a pan-coronavirus lipopeptide inhibitor potently inhibiting virion fusion.iScience · 2026Article
- Mutations to the HCoV-229E spike have counterbalancing effects on serum antibody neutralization and receptor binding.bioRxiv : the preprint server for biology · 2026Article
- Enhancing the solubility of SARS-CoV-2 inhibitors to increase future prospects for clinical development.Journal of virology · 2025Article
- Structures of HCoV-OC43 HR1 Domain in Complex with Cognate HR2 or Analogue EK1 Peptide.Viruses · 2025Article
- Article
- Structural conservation among variants of the SARS-CoV-2 spike postfusion bundle.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Heptad stereotypy, S/Q layering, and remote origin of the SARS-CoV-2 fusion core.Virus evolution · 2022Article
- Peptide-Based Dual HIV and Coronavirus Entry Inhibitors.Advances in experimental medicine and biology · 2022Review
- A Review of Human Coronaviruses' Receptors: The Host-Cell Targets for the Crown Bearing Viruses.Molecules (Basel, Switzerland) · 2021Review
- Molecular scaffolds from mother nature as possible lead compounds in drug design and discovery against coronaviruses: A landscape analysis of published literature and molecular docking studies.Microbial pathogenesis · 2021Review
- Possible Targets of Pan-Coronavirus Antiviral Strategies for Emerging or Re-Emerging Coronaviruses.Microorganisms · 2021Review
- Inflammation, immunity and potential target therapy of SARS-COV-2: A total scale analysis review.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2021Review
- Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodies.Cellular and molecular life sciences : CMLS · 2021Article
- Natural and Nature-Derived Products Targeting Human Coronaviruses.Molecules (Basel, Switzerland) · 2021Review
- Article
- A pan-coronavirus fusion inhibitor targeting the HR1 domain of human coronavirus spike.Science advances · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Human coronavirus 229E (HCoV-229E) usually causes mild upper respiratory infections in heathy adults, but may lead to severe complications or mortality in individuals with weakened immune systems. Virus entry of HCoV-229E is mediated by its spike (S) protein, where the S1 domain facilitates attachment to host cells and the S2 domain is involved in subsequent fusion of the virus and host membranes. During the fusion process, two heptad repeats, HR1 and HR2, in the S2 domain assemble into a six-helix membrane-fusion structure termed the fusion core. Here, the complete fusion-core structure of HCoV-229E has been determined at 1.86 Å resolution, representing the most complete post-fusion conformation thus far among published human alphacoronavirus (α-HCoV) fusion-core structures. The overall structure of the HCoV-229E fusion core is similar to those of SARS, MERS and HCoV-NL63, but the packing of its 3HR1 core differs from those of SARS and MERS in that it contains more noncanonical `x' and `da' layers. Side-by-side electrostatic surface comparisons reveal that the electrostatic surface potentials are opposite in α-HCoVs and β-HCoVs at certain positions and that the HCoV-229E surface also appears to be the most hydrophobic among the various HCoVs. In addition to the highly conserved hydrophobic interactions between HR1 and HR2, some polar and electrostatic interactions are also well preserved across different HCoVs. This study adds to the structural profiling of HCoVs to aid in the structure-based design of pan-coronavirus small molecules or peptides to inhibit viral fusion.
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