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The Free Fatty Acid-Binding Pocket is a Conserved Hallmark in Pathogenic β-Coronavirus Spike Proteins from SARS-CoV to Omicron
Christine Toelzer; Kapil Gupta; Sathish K.N. Yadav; Lorna Hodgson; Maia Kavanagh Williamson; Dora Buzas; Ufuk Borucu; Kyle Powers; Richard Stenner; Kate Vasileiou; Frederik Garzoni; Daniel Fitzgerald; Gerard Lambeau; Andrew D. Davidson; Paul Verkade; Martin Frank; Imre Berger; Christiane Schaffitzel.
Afiliación
  • Christine Toelzer; University of Bristol, Bristol, UK
  • Kapil Gupta; University of Bristol
  • Sathish K.N. Yadav; University of Bristol, Bristol, UK
  • Lorna Hodgson; University of Bristol, Bristol, UK
  • Maia Kavanagh Williamson; University of Bristol, Bristol, UK
  • Dora Buzas; University of Bristol, Bristol, UK
  • Ufuk Borucu; University of Bristol, Bristol, UK
  • Kyle Powers; University of Bristol, Bristol, UK
  • Richard Stenner; University of Bristol, Bristol, UK
  • Kate Vasileiou; University of Bristol, Bristol, UK
  • Frederik Garzoni; Imophoron LTD, Bristol, UK
  • Daniel Fitzgerald; Halo Therapeutics LTD, Bristol, UK
  • Gerard Lambeau; Institut de Pharmacologie Moleculaire et Cellulaire, Valbonne, France
  • Andrew D. Davidson; University of Bristol
  • Paul Verkade; University of Bristol
  • Martin Frank; Biognos AB, Goteborg, Sweden
  • Imre Berger; University of Bristol
  • Christiane Schaffitzel; University of Bristol
Preprint en En | PREPRINT-BIORXIV | ID: ppbiorxiv-489083
ABSTRACT
As COVID-19 persists, severe acquired 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 {beta}-coronaviruses ({beta}-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 LA-free. 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 {beta}-CoV infection and replication, highlighting potential antiviral strategies. One-Sentence SummaryFree fatty acid-binding is conserved in pathogenic {beta}-coronavirus S proteins and suppresses viral infection and replication.
Licencia
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Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Idioma: En Año: 2022 Tipo del documento: Preprint
Texto completo: 1 Colección: 09-preprints Base de datos: PREPRINT-BIORXIV Idioma: En Año: 2022 Tipo del documento: Preprint