ArticleScience advances2022
The free fatty acid-binding pocket is a conserved hallmark in pathogenic β-coronavirus spike proteins from SARS-CoV to Omicron.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Behind the membranous curtain-lipid dynamics and functions in coronaviral replication.Journal of virology · 2026Review
- AI-guided prefusion stabilization of the human coronavirus OC43 spike protein enables universal embecovirus antigen design.PLoS pathogens · 2026Article
- Cryo-EM structure of locked spike glycoprotein from bat SARS-like coronavirus WIV1, molecular dynamics and biophysics across host range.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Development of an inactivated viral transport medium for diagnostic testing in low-resource countries.Narra J · 2025Article
- A SARS-CoV-2 entry inhibitor trimerizes to lock the spike protein in a closed conformation.bioRxiv : the preprint server for biology · 2025Article
- Article
- Structures and receptor binding activities of merbecovirus spike proteins reveal key signatures for human DPP4 adaptation.Science advances · 2025Article
- Metabolic features of patients with repeated Omicron infections highlight new targets for therapeutic intervention.Scientific reports · 2025Article
- 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
- In Silico Discovery of a Novel Antiviral Scaffold for SARS-CoV‑2 Targeting the Spike Glycoprotein through the Fatty Acid Binding Pocket.ACS omega · 2025Article
- Article
- SARS-related coronavirus S-protein structures reveal synergistic RBM interactions underpinning high-affinity human ACE2 binding.Science advances · 2025Article
- Expression and Purification of SARS-related Spike Glycoproteins for Cryo-EM Analysis.Current protocols · 2025Article
- Disrupting SARS-CoV-2 Spike Protein Activity: A Virtual Screening and Binding Assay Study.International journal of molecular sciences · 2024Article
- Antibodies utilizing VL6-57 light chains target a convergent cryptic epitope on SARS-CoV-2 spike protein and potentially drive the genesis of Omicron variants.Nature communications · 2024Article
- Hybrid immunity to SARS-CoV-2 arises from serological recall of IgG antibodies distinctly imprinted by infection or vaccination.Cell reports. Medicine · 2024Article
- Structural determinants of spike infectivity in bat SARS-like coronaviruses RsSHC014 and WIV1.Journal of virology · 2024Article
- Variation in structural motifs within SARS-related coronavirus spike proteins.PLoS pathogens · 2024Article
- Exploring Binding Pockets in the Conformational States of the SARS-CoV-2 Spike Trimers for the Screening of Allosteric Inhibitors Using Molecular Simulations and Ensemble-Based Ligand Docking.International journal of molecular sciences · 2024Article
- Can essential fatty acids (EFAs) prevent and ameliorate post-COVID-19 long haul manifestations?Lipids in health and disease · 2024Review
Corrections and comments
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Authors and funding
20 authors at 5 institutions in 3 countries.
Funding
Abstract
As coronavirus disease 2019 (COVID-19) persists, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) emerge, accumulating spike (S) glycoprotein mutations. S receptor binding domain (RBD) comprises a free fatty acid (FFA)-binding pocket. FFA binding stabilizes a locked S conformation, interfering with virus infectivity. We provide evidence that the pocket is conserved in pathogenic β-coronaviruses (β-CoVs) infecting humans. SARS-CoV, MERS-CoV, SARS-CoV-2, and VOCs bind the essential FFA linoleic acid (LA), while binding is abolished by one mutation in common cold-causing HCoV-HKU1. In the SARS-CoV S structure, LA stabilizes the locked conformation, while the open, infectious conformation is devoid of LA. Electron tomography of SARS-CoV-2-infected cells reveals that LA treatment inhibits viral replication, resulting in fewer deformed virions. Our results establish FFA binding as a hallmark of pathogenic β-CoV infection and replication, setting the stage for FFA-based antiviral strategies to overcome COVID-19.
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