Literature detail

Insights on cross-species transmission of SARS-CoV-2 from structural modeling.

João P G L M Rodrigues1 Susana Barrera-Vilarmau2 João M C Teixeira3 Marija Sorokina4 Elizabeth Seckel5 Panagiotis L Kastritis4 Michael Levitt1
Affiliations 5 institutions
  1. Department of Structural Biology, Stanford University School of Medicine, Stanford, California, United States of America.
  2. Institute of Advanced Chemistry of Catalonia (IQAC), CSIC, Barcelona, Spain.
  3. Program in Molecular Medicine, The Hospital for Sick Children, Toronto, Ontario, Canada.
  4. ZIK HALOMEM & Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Biozentrum, Halle (Saale), Germany.
  5. Department of Obstetrics and Gynecology, Stanford University School of Medicine, Stanford, California, United States of America.
PMID 33270653 2020 PLoS Comput Biol eng epublish
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Article

Publication summary

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is responsible for the ongoing global pandemic that has infected more than 31 million people in more than 180 countries worldwide. Like other coronaviruses, SARS-CoV-2 is thought to have been transmitted to humans from wild animals. Given the scale and widespread geographical distribution of the current pandemic and confirmed cases of cross-species transmission, the question of the extent to which this transmission is possible emerges, as well as what molecular features distinguish susceptible from non-susceptible animal species. Here, we investigated the structural properties of several ACE2 orthologs bound to the SARS-CoV-2 spike protein. We found that species known not to be susceptible to SARS-CoV-2 infection have non-conservative mutations in several ACE2 amino acid residues that disrupt key polar and charged contacts with the viral spike protein. Our models also allow us to predict affinity-enhancing mutations that could be used to design ACE2 variants for therapeutic purposes. Finally, our study provides a blueprint for modeling viral-host protein interactions and highlights several important considerations when designing these computational studies and analyzing their results.

COVID-19 SARS-CoV-2 Angiotensin-Converting Enzyme 2 Animals Binding Sites Computational Biology Conserved Sequence Genetic Predisposition to Disease Host-Pathogen Interactions Humans Molecular Dynamics Simulation Mutation Spike Glycoprotein, Coronavirus Viral Zoonoses spike protein, SARS-CoV-2

Structured evidence records

Evidence records

3 total
1 records
Extraction confidence 0.80
Key finding

Computational analysis of ACE2 orthologs indicated molecular determinants that influence SARS-CoV-2 infection susceptibility among different non-human animal species, supporting potential animal-to-animal transmission.

Virus
Host
Location
Not specified
Supporting text

We investigated the structural properties of several ACE2 orthologs bound to the SARS-CoV-2 spike protein to understand molecular features that distinguish susceptible from non-susceptible animal species, providing insights into confirmed cases of cross-species transmission.

Method
structural modeling; ACE2 ortholog analysis
Study design
computational structural modeling
Transmission direction
animal-to-animal
1 records
Extraction confidence 0.90
Key finding

Non-susceptible animal species display ACE2 mutations that weaken interactions with the SARS-CoV-2 spike protein, suggesting molecular adaptation determinants of host susceptibility.

Virus
Host
Not specified
Location
Not specified
Supporting text

Species known not to be susceptible to SARS-CoV-2 infection have non-conservative mutations in several ACE2 amino acid residues that disrupt key polar and charged contacts with the viral spike protein.

Genes or proteins
ACE2; spike protein
Receptors
ACE2
Mechanism types
receptor_binding; cell_entry; host_range_determination
1 records
Extraction confidence 0.95
Key finding

Structural analysis showed that variations in ACE2 residues alter binding interfaces with SARS-CoV-2 spike, explaining differences in receptor compatibility and susceptibility among animal species.

Virus
Host
Location
Not specified
Supporting text

We investigated the structural properties of several ACE2 orthologs bound to the SARS-CoV-2 spike protein. Species known not to be susceptible to SARS-CoV-2 infection have non-conservative mutations in several ACE2 amino acid residues that disrupt key polar and charged contacts with the viral spike protein.

Method
structural modeling
Receptors
ACE2