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Structure paper

TitleCryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range.
Journal, issue, pagesPLoS Pathog, Vol. 19, Issue 4, Page e1011206, Year 2023
Publish dateApr 5, 2023
AuthorsDongchun Ni / Priscilla Turelli / Bertrand Beckert / Sergey Nazarov / Emiko Uchikawa / Alexander Myasnikov / Florence Pojer / Didier Trono / Henning Stahlberg / Kelvin Lau /
PubMed AbstractInvestigation of potential hosts of the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is crucial to understanding future risks of spillover and spillback. SARS-CoV-2 has been reported ...Investigation of potential hosts of the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) is crucial to understanding future risks of spillover and spillback. SARS-CoV-2 has been reported to be transmitted from humans to various animals after requiring relatively few mutations. There is significant interest in describing how the virus interacts with mice as they are well adapted to human environments, are used widely as infection models and can be infected. Structural and binding data of the mouse ACE2 receptor with the Spike protein of newly identified SARS-CoV-2 variants are needed to better understand the impact of immune system evading mutations present in variants of concern (VOC). Previous studies have developed mouse-adapted variants and identified residues critical for binding to heterologous ACE2 receptors. Here we report the cryo-EM structures of mouse ACE2 bound to trimeric Spike ectodomains of four different VOC: Beta, Omicron BA.1, Omicron BA.2.12.1 and Omicron BA.4/5. These variants represent the oldest to the newest variants known to bind the mouse ACE2 receptor. Our high-resolution structural data complemented with bio-layer interferometry (BLI) binding assays reveal a requirement for a combination of mutations in the Spike protein that enable binding to the mouse ACE2 receptor.
External linksPLoS Pathog / PubMed:37018380 / PubMed Central
MethodsEM (single particle)
Resolution2.92 - 4.4 Å
Structure data

15588

8aqs

EMDB-15588, PDB-8aqs:
BA.4/5 SARS-CoV-2 Spike bound to human ACE2 (local)
Method: EM (single particle) / Resolution: 2.92 Å

15589

8aqt

EMDB-15589, PDB-8aqt:
Beta SARS-CoV-2 Spike bound to mouse ACE2 (local)
Method: EM (single particle) / Resolution: 4.4 Å

15590

8aqu

EMDB-15590, PDB-8aqu:
BA.1 SARS-CoV-2 Spike bound to mouse ACE2 (local)
Method: EM (single particle) / Resolution: 3.22 Å

15591

8aqv

EMDB-15591, PDB-8aqv:
BA.2.12.1 SARS-CoV-2 Spike bound to mouse ACE2 (local)
Method: EM (single particle) / Resolution: 2.96 Å

15592

8aqw

EMDB-15592, PDB-8aqw:
BA.4/5 SARS-CoV-2 Spike bound to mouse ACE2 (local)
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
  • enterobacteria phage t4 (virus)
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN / SARS-COV2 / omicron / Spike / RBD / mouse / ACE2 / ANTIVIRAL PROTEIN / BA4/5 / Beta / BA.1 / BA2.12.1

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