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TitleNeutralization of SARS-CoV-2 by Destruction of the Prefusion Spike.
Journal, issue, pagesCell Host Microbe, Vol. 28, Issue 3, Page 445-454.e6, Year 2020
Publish dateSep 9, 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 / Piyada 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 linksCell Host Microbe / PubMed:32585135 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.42 - 4.36 Å
Structure data

10863

6yor

EMDB-10863, PDB-6yor:
Structure of the SARS-CoV-2 spike S1 protein in complex with CR3022 Fab
Method: EM (single particle) / Resolution: 3.3 Å

11119

6z97

EMDB-11119, PDB-6z97:
Structure of the prefusion SARS-CoV-2 spike glycoprotein
Method: EM (single particle) / Resolution: 3.4 Å

PDB-6yla:
Crystal structure of the SARS-CoV-2 receptor binding domain in complex with CR3022 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

PDB-6ym0:
Crystal structure of the SARS-CoV-2 receptor binding domain in complex with CR3022 Fab (crystal form 1)
Method: X-RAY DIFFRACTION / Resolution: 4.36 Å

Chemicals

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-MLI:
MALONATE ION

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-PG0:
2-(2-METHOXYETHOXY)ETHANOL / inhibitor, precipitant*YM

ChemComp-HOH:
WATER

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
  • enterobacteria phage t4 (virus)
KeywordsVIRAL PROTEIN / SARS-CoV-2 Spike protein / RBD / CR3022 / complex / SARS-CoV-2 / receptor binding domain (RBD) / Vagabond / SARS-CoV-2 Spike glycoprotein

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