Literature detail

Comparative analyses of ACE2 and TMPRSS2 gene: Implications for the risk to which vertebrate animals are susceptible to SARS-CoV-2.

Chen Huang1 Yu Jiang2 Jie Yan3
Affiliations 3 institutions
  1. Department of Veterinary Science, University of Kentucky, Lexington, Kentucky, USA.
  2. Division of Epidemiology, Biostatistics, and Environmental Health, School of Public Health, University of Memphis, Memphis, Tennessee, USA.
  3. Department of Diagnosis, School of Medicine, Cheeloo College of Medicine, Shandong University, Jinan, Shandong, China.
PMID 33974296 2021 J Med Virol eng ppublish
PubMed DOI Browse context

Article

Publication summary

Along with the control and prevention of coronavirus disease 2019 transmission, infected animals might have potential to carry the virus to spark new outbreaks. However, very few studies explore the susceptibility of animals to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Viral attachment as a crucial step for cross-species infection requires angiotensin-converting enzyme 2 (ACE2) as a receptor and depends on TMPRSS2 protease activity. Here, we searched the genomes of metazoans from different classes using an extensive BLASTP survey and found ACE2 and TMPRSS2 occur in vertebrates, but some vertebrates lack Tmprss2. We identified 6 amino acids among 25 known human ACE2 residues are highly associated with the binding of ACE2 to SARS-CoV-2 (p value < .01) by Fisher exact test, and following this, calculated the probability of viral attachment within each species by the randomForest function from R randomForest library. Furthermore, we observed that Ace2 selected from seven animals based on the above analysis lack the hydrophobic contacts identified on human ACE2, indicating less affinity of SARS-CoV-2 to Ace2 in animals than humans. Finally, the alignment of 3D structure between human ACE2 and other animals by I-TASSER and TM-align displayed a reasonable structure for viral attachment within these species. Taken together, our data may shed light on the human-to-animal transmission of SARS-CoV-2.

ACE2 infection livestock SARS-CoV-2 TMPRSS2 Host-Pathogen Interactions Angiotensin-Converting Enzyme 2 Animals COVID-19 Disease Susceptibility Genetic Predisposition to Disease Humans Receptors, Virus SARS-CoV-2 Serine Endopeptidases Spike Glycoprotein, Coronavirus Vertebrates Virus Attachment

Structured evidence records

Evidence records

3 total
1 records
Extraction confidence 0.70
Key finding

Comparative genomic and structural analyses of ACE2 and TMPRSS2 suggest sequence and structural differences among vertebrates influence SARS-CoV-2 receptor compatibility.

Virus
Host
Location
Not specified
Supporting text

We searched the genomes of metazoans from different classes using an extensive BLASTP survey and found ACE2 and TMPRSS2 occur in vertebrates... alignment of 3D structure between human ACE2 and other animals by I-TASSER and TM-align displayed a reasonable structure for viral attachment within these species.

Genes or proteins
ACE2; TMPRSS2
Analysis methods
comparative genomics; BLASTP survey; protein structure alignment
1 records
Extraction confidence 0.90
Key finding

Six ACE2 amino acid residues were found to differ between humans and other vertebrates, potentially reducing SARS-CoV-2 binding affinity and influencing cross-species adaptation.

Virus
Host
Not specified
Location
Not specified
Supporting text

We identified 6 amino acids among 25 known human ACE2 residues highly associated with the binding of ACE2 to SARS-CoV-2 and observed that Ace2 from seven animals lacked hydrophobic contacts identified on human ACE2, indicating less affinity of SARS-CoV-2 to Ace2 in animals than humans.

Genes or proteins
ACE2; TMPRSS2; Spike Glycoprotein
Receptors
ACE2
Host factors
TMPRSS2
Mechanism types
receptor_binding; cell_entry; host_factor_interaction
1 records
Extraction confidence 0.95
Key finding

SARS-CoV-2 uses ACE2 as a receptor and TMPRSS2 for entry, with animal ACE2 sequences showing reduced hydrophobic contacts and lower predicted binding affinity compared to human ACE2.

Virus
Host
Not specified
Location
Not specified
Supporting text

Viral attachment as a crucial step for cross-species infection requires angiotensin-converting enzyme 2 (ACE2) as a receptor and depends on TMPRSS2 protease activity. We identified 6 amino acids among 25 known human ACE2 residues highly associated with binding of ACE2 to SARS-CoV-2 and observed that ACE2 selected from seven animals lack the hydrophobic contacts identified on human ACE2, indicating less affinity of SARS-CoV-2 to ACE2 in animals than humans.

Method
BLASTP survey; Fisher exact test; randomForest analysis; 3D structural alignment using I-TASSER and TM-align
Receptors
ACE2
Host factors
TMPRSS2