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TitleNeutralization of SARS-CoV-2 by Destruction of the Prefusion Spike.
Journal, issue, pagesCell Host Microbe, Year 2020
Publish dateJun 19, 2020
AuthorsJiandong Huo / Yuguang Zhao / Jingshan Ren / Daming Zhou / Helen M E Duyvesteyn / Helen M Ginn / Loic Carrique / Tomas Malinauskas / Reinis R Ruza / Pranav N M Shah / Tiong Kit Tan / Pramila Rijal / Naomi Coombes / Kevin R Bewley / Julia A Tree / Julika Radecke / Neil G Paterson / Piyasa Supasa / Juthathip Mongkolsapaya / Gavin R Screaton / Miles Carroll / Alain Townsend / Elizabeth E Fry / Raymond J Owens / David I Stuart /
PubMed AbstractThere are as yet no licensed therapeutics for the COVID-19 pandemic. The causal coronavirus (SARS-CoV-2) binds host cells via a trimeric spike whose receptor binding domain (RBD) recognizes ...There are as yet no licensed therapeutics for the COVID-19 pandemic. The causal coronavirus (SARS-CoV-2) binds host cells via a trimeric spike whose receptor binding domain (RBD) recognizes angiotensin-converting enzyme 2, initiating conformational changes that drive membrane fusion. We find that the monoclonal antibody CR3022 binds the RBD tightly, neutralizing SARS-CoV-2, and report the crystal structure at 2.4 Å of the Fab/RBD complex. Some crystals are suitable for screening for entry-blocking inhibitors. The highly conserved, structure-stabilizing CR3022 epitope is inaccessible in the prefusion spike, suggesting that CR3022 binding facilitates conversion to the fusion-incompetent post-fusion state. Cryogenic electron microscopy (cryo-EM) analysis confirms that incubation of spike with CR3022 Fab leads to destruction of the prefusion trimer. Presentation of this cryptic epitope in an RBD-based vaccine might advantageously focus immune responses. Binders at this epitope could be useful therapeutically, possibly in synergy with an antibody that blocks receptor attachment.
External linksPubMed:32585135 / Publisher's page
KeywordsVIRAL PROTEIN / SARS-CoV-2 Spike protein / RBD / CR3022 / complex / SARS-CoV-2 Spike glycoprotein
MethodsEM (single particle)
Resolution3.3 - 3.4 A
Structure data

EMDB-10863:
Structure of the SARS-CoV-2 spike S1 protein in complex with CR3022 Fab

PDB-6yor:
Structure of the SARS-CoV-2 spike S1 protein in complex with CR3022 Fab

PDB-6z97:
Structure of the prefusion SARS-CoV-2 spike glycoprotein

Chemicals

ChemComp-NAG:
Unknown entry

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
  • enterobacteria phage t4 (bacteriophage)

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