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Computers in biology and medicine2021; 141; 105017; doi: 10.1016/j.compbiomed.2021.105017

Computational insights into differential interaction of mammalian angiotensin-converting enzyme 2 with the SARS-CoV-2 spike receptor binding domain.

Abstract: The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the COVID-19 pandemic. Angiotensin-converting enzyme 2 (ACE2) has been identified as the host cell receptor that binds to the receptor-binding domain (RBD) of the SARS-COV-2 spike protein and mediates cell entry. Because the ACE2 proteins are widely available in mammals, it is important to investigate the interactions between the RBD and the ACE2 of other mammals. Here we analyzed the sequences of ACE2 proteins from 16 mammals, predicted the structures of ACE2-RBD complexes by homology modeling, and refined the complexes using molecular dynamics simulation. Analyses on sequence, structure, and dynamics synergistically provide valuable insights into the interactions between ACE2 and RBD. The analysis outcomes suggest that the ACE2 of bovine, cat, and panda form strong binding interactions with RBD, while in the cases of rat, least horseshoe bat, horse, pig, mouse, and civet, the ACE2 proteins interact weakly with RBD.
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Publication Date: 2021-11-03 PubMed ID: 34758907PubMed Central: PMC8565036DOI: 10.1016/j.compbiomed.2021.105017Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This study uses computational models to investigate how a key protein on the SARS-CoV-2 virus interacts with the same protein in a variety of mammals. Results suggest this interaction is stronger in certain species, such as bovines, cats, and pandas, compared to others like rats, bats, horses, pigs, mice, and civets.

Methodology

  • The researchers compiled the sequences of a protein known as angiotensin-converting enzyme 2 (ACE2) from 16 different mammals. This protein is a primary point of interaction between host cells and the SARS-CoV-2 virus, which causes COVID-19.
  • Using these sequences, the team predicted and refined the structures of complexes between the virus’s receptor-binding domain (RBD) and ACE2 in each mammal. They used a process known as homology modeling, which compares sequences to predict the three-dimensional molecular structure.
  • After producing these models, the researchers then refined them using molecular dynamics simulation. This is a computer simulation method for studying the physical movements of atoms and molecules, allowing for the analysis of the interaction between RBD and ACE2.

Findings

  • The ACE2 of bovine, cat, and panda mammals exhibited strong binding interactions with the RBD protein of SARS-CoV-2. This indicates a possible high susceptibility of these species to the virus.
  • Conversely, the ACE2 proteins of rat, least horseshoe bat, horse, pig, mouse, and civet displayed weakly-interacting relationships with RBD, which might suggest a lower likelihood of successful infection with SARS-CoV-2.

Implications

  • This study offers insights into which animals may be particularly vulnerable or resistant to SARS-CoV-2 infection, based on how the virus’s spike protein interacts with specific host proteins.
  • These findings may help guide efforts to monitor and control the spread of the virus in animal populations. They may also inform future research into the spillover of the virus from animals to humans.

Cite This Article

APA
Lupala CS, Kumar V, Su XD, Wu C, Liu H. (2021). Computational insights into differential interaction of mammalian angiotensin-converting enzyme 2 with the SARS-CoV-2 spike receptor binding domain. Comput Biol Med, 141, 105017. https://doi.org/10.1016/j.compbiomed.2021.105017

Publication

Computers in biology and medicine
ISSN: 1879-0534
NlmUniqueID: 1250250
Country: United States
Language: English
Volume: 141
Pages: 105017
PII: S0010-4825(21)00811-8

Researcher Affiliations

Lupala, Cecylia Severin
  • Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China. Electronic address: cecylia@csrc.ac.cn.
Kumar, Vikash
  • Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China. Electronic address: vikash@csrc.ac.cn.
Su, Xiao-Dong
  • State Key Laboratory of Protein and Plant Gene Research and Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, 100871, People's Republic of China.
Wu, Chun
  • Department of Chemistry & Biochemistry and Molecular & Cellular Biosciences, Rowan University, Glassboro, NJ, 08028, USA.
Liu, Haiguang
  • Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China; Physics Department, Beijing Normal University, Haidian, Beijing, 100875, People's Republic of China.

MeSH Terms

  • Angiotensin-Converting Enzyme 2
  • Animals
  • COVID-19
  • Cattle
  • Chiroptera
  • Horses
  • Humans
  • Mice
  • Molecular Dynamics Simulation
  • Pandemics
  • Protein Binding
  • Rats
  • SARS-CoV-2
  • Spike Glycoprotein, Coronavirus
  • Swine

Conflict of Interest Statement

None Declared.

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