RT Journal Article
SR Electronic
T1 SARS-CoV-2 spike protein predicted to form stable complexes with host receptor protein orthologues from mammals, but not fish, birds or reptiles
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.05.01.072371
DO 10.1101/2020.05.01.072371
A1 SD Lam
A1 N Bordin
A1 VP Waman
A1 HM Scholes
A1 P Ashford
A1 N Sen
A1 L van Dorp
A1 C Rauer
A1 NL Dawson
A1 CSM Pang
A1 M Abbasian
A1 I Sillitoe
A1 SJL Edwards
A1 F Fraternali
A1 JG Lees
A1 JM Santini
A1 CA Orengo
YR 2020
UL http://biorxiv.org/content/early/2020/05/11/2020.05.01.072371.abstract
AB The coronavirus disease 2019 (COVID-19) global pandemic is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). SARS-CoV-2 has a zoonotic origin and was transmitted to humans via an undetermined intermediate host, leading to infections in humans and other mammals. To enter host cells, the viral spike protein binds to its receptor, angiotensin-converting enzyme 2 (ACE2), and is then processed by transmembrane protease serine 2 (TMPRSS2). Whilst receptor binding contributes to the viral host range, changes in energy of spike protein:ACE2 complexes in other animals have not been widely explored. Here, we analyse interactions between the spike protein and orthologues of ACE2 and TMPRSS2 from a broad range of 215 vertebrate species. Using models of spike protein:ACE2 orthologue complexes, we calculated their changes in energy, correlated to mammalian COVID-19 infection data. Across vertebrates, mutations are predicted to have more impact on the function of ACE2 than TMPRSS2. Finally, we provide phylogenetic analysis demonstrating that human SARS-CoV-2 strains have been isolated in animals. Our results suggest that SARS-CoV-2 can infect a broad range of mammals, but not fish, birds or reptiles. Susceptible animals could serve as reservoirs of the virus, necessitating careful ongoing animal management and surveillance.Competing Interest StatementThe authors have declared no competing interest.