OmniVira

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

Cecylia Severin Lupala1 Vikash Kumar2 Xiao-Dong Su3 Chun Wu4 Haiguang Liu5,6
Affiliations 6 institutions
  1. Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China. Electronic address: [email protected].
  2. Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China. Electronic address: [email protected].
  3. State Key Laboratory of Protein and Plant Gene Research and Biomedical Pioneering Innovation Center (BIOPIC), Peking University, Beijing, 100871, People's Republic of China.
  4. Department of Chemistry & Biochemistry and Molecular & Cellular Biosciences, Rowan University, Glassboro, NJ, 08028, USA.
  5. Complex Systems Division, Beijing Computational Science Research Center, Haidian, Beijing, 100193, People's Republic of China
  6. Physics Department, Beijing Normal University, Haidian, Beijing, 100875, People's Republic of China.
PMID34758907 DOI10.1016/j.compbiomed.2021.105017 Year2022 Journal Computers in biology and medicine Comput Biol Med Languageeng Publication statusActive
Active Last checked 2026-10-04 03:30:36 Source: NCBI PubMed

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.

Supporting text Virus Host Location
ACE2 55 Homology modeling 3 Molecular dynamics 11 RBD 13 SARS-CoV-2 556 Chiroptera 376 COVID-19 427 Angiotensin-Converting Enzyme 2 178 Animals 1981 Cattle 129 Horses 52 Humans 1455 Mice 256 Molecular Dynamics Simulation 21 Pandemics 109 Protein Binding 194 Rats 73 SARS-CoV-2 456 Spike Glycoprotein, Coronavirus 276 Swine 261 spike protein, SARS-CoV-2 158

Evidence records

1 total
Functional Mechanism
1 records · 1 evidence types
Evidence type Receptor Usage
1 records
OVE5362 Receptor Usage
Key finding

ACE2 is identified as the host cell receptor that binds to the SARS-CoV-2 spike receptor-binding domain and mediates cell entry.

Virus
Severe acute respiratory syndrome coronavirus 2
Host
host cell Experimental system
Location
Not specified
Supporting text

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.

Method
binding analysis | computational modeling | structural analysis
Receptors
ACE2
Host factors
spike protein