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Literature detail

Structure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2.

Antoni G Wrobel1 Donald J Benton2 Pengqi Xu3,4 Lesley J Calder5 Annabel Borg6 Chloë Roustan6 Stephen R Martin3 Peter B Rosenthal5 John J Skehel3 Steven J Gamblin7
Affiliations 7 institutions
  1. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. [email protected].
  2. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. [email protected].
  3. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
  4. Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, Guangdong, China.
  5. Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, NW1 1AT, London, UK.
  6. Structural Biology Science Technology Platform, Francis Crick Institute, NW1 1AT, London, UK.
  7. Structural Biology of Disease Processes Laboratory, Francis Crick Institute, NW1 1AT, London, UK. [email protected].
PMID 33547281 2021 Nat Commun eng epublish
PubMed DOI Browse context

Article

Publication summary

Coronaviruses of bats and pangolins have been implicated in the origin and evolution of the pandemic SARS-CoV-2. We show that spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind strongly to human and pangolin ACE2 receptors. We also report the cryo-EM structure of a Pangolin-CoV spike protein and show it adopts a fully-closed conformation and that, aside from the Receptor-Binding Domain, it resembles the spike of a bat coronavirus RaTG13 more than that of SARS-CoV-2.

Evolution, Molecular Angiotensin-Converting Enzyme 2 Animals Binding, Competitive COVID-19 Cryoelectron Microscopy Humans Models, Molecular Pandemics Pangolins Protein Binding Protein Domains SARS-CoV-2 Spike Glycoprotein, Coronavirus ACE2 protein, human spike protein, SARS-CoV-2

Structured evidence records

Evidence records

5 total
Genomic Evolution 2 records
Genomic Evolution Extraction confidence 0.75
Key finding

Structural comparison revealed that the Pangolin-CoV spike protein is more similar to the bat coronavirus RaTG13 spike than to SARS-CoV-2, highlighting genomic and structural relationships relevant to SARS-CoV-2 evolution.

Virus
SARSr-CoV
Location
Not specified
Supporting text

We also report the cryo-EM structure of a Pangolin-CoV spike protein and show it adopts a fully-closed conformation and that, aside from the Receptor-Binding Domain, it resembles the spike of a bat coronavirus RaTG13 more than that of SARS-CoV-2.

Genes or proteins
spike glycoprotein
Analysis methods
structural analysis; comparative genomic analysis
Genomic Evolution Extraction confidence 0.75
Key finding

Bat and pangolin coronaviruses exhibit genetic relationships suggesting their involvement in the evolutionary origin of SARS-CoV-2.

Virus
SARS-CoV-2
Location
Not specified
Supporting text

Coronaviruses of bats and pangolins have been implicated in the origin and evolution of the pandemic SARS-CoV-2.

Genes or proteins
spike glycoprotein
Analysis methods
comparative genomic analysis
Receptor Usage 2 records
Receptor Usage Extraction confidence 0.95
Key finding

Guangdong Pangolin-CoV spike protein exhibits strong binding to ACE2 receptors from both humans and pangolins.

Virus
SARSr-CoV
Location
Not specified
Supporting text

Spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind strongly to human and pangolin ACE2 receptors.

Method
binding assay; cryo-EM structure analysis
Receptors
ACE2
Receptor Usage Extraction confidence 0.95
Key finding

Guangdong Pangolin-CoV spike protein binds strongly to ACE2 receptors from pangolins.

Virus
SARSr-CoV
Location
Not specified
Supporting text

Spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind strongly to human and pangolin ACE2 receptors.

Method
binding assay; cryo-EM structure analysis
Receptors
ACE2
Molecular Adaptation 1 records
Molecular Adaptation Extraction confidence 0.85
Key finding

Pangolin-CoV spike glycoproteins strongly bind human and pangolin ACE2 receptors, indicating molecular adaptation relevant to cross-species host interaction and evolution of SARS-CoV-2.

Virus
SARSr-CoV
Host
Not specified
Location
Not specified
Supporting text

We show that spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind strongly to human and pangolin ACE2 receptors.

Genes or proteins
spike
Receptors
ACE2
Mechanism types
receptor_binding; cell_entry; host_specific_adaptation