tetano
Editor, Senior Moderator
Proc Natl Acad Sci U S A
. 2024 Aug 6;121(32):e2322600121.
doi: 10.1073/pnas.2322600121. Epub 2024 Jul 31. Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses
Wei Zhang[SUP] #[/SUP][SUP] 1 2 [/SUP], Ke Shi[SUP] #[/SUP][SUP] 3 [/SUP], Fu-Chun Hsueh[SUP] 1 2 [/SUP], Alise Mendoza[SUP] 1 2 [/SUP], Gang Ye[SUP] 1 2 [/SUP], Linfen Huang[SUP] 1 2 [/SUP], Stanley Perlman[SUP] 4 [/SUP], Hideki Aihara[SUP] 3 [/SUP], Fang Li[SUP] 1 2 [/SUP]
Affiliations
The animal origin of SARS-CoV-2 remains elusive, lacking a plausible evolutionary narrative that may account for its emergence. Its spike protein resembles certain segments of BANAL-236 and RaTG13, two bat coronaviruses considered possible progenitors of SARS-CoV-2. Additionally, its spike contains a furin motif, a common feature of rodent coronaviruses. To explore the possible involvement of rodents in the emergence of SARS-CoV-2 spike, we examined the crystal structures of the spike receptor-binding domains (RBDs) of BANAL-236 and RaTG13 each complexed with mouse receptor ACE2. Both RBDs have residues at positions 493 and 498 that align well with two virus-binding hotspots on mouse ACE2. Our biochemical evidence supports that both BANAL-236 and RaTG13 spikes can use mouse ACE2 as their entry receptor. These findings point to a scenario in which these bat coronaviruses may have coinfected rodents, leading to a recombination of their spike genes and a subsequent acquisition of a furin motif in rodents, culminating in the emergence of SARS-CoV-2.
Keywords: SARS-CoV-2; X-ray crystallography; angiotensin-converting enzyme 2 (ACE2); receptor-binding domain (RBD); spike protein.
. 2024 Aug 6;121(32):e2322600121.
doi: 10.1073/pnas.2322600121. Epub 2024 Jul 31. Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses
Wei Zhang[SUP] #[/SUP][SUP] 1 2 [/SUP], Ke Shi[SUP] #[/SUP][SUP] 3 [/SUP], Fu-Chun Hsueh[SUP] 1 2 [/SUP], Alise Mendoza[SUP] 1 2 [/SUP], Gang Ye[SUP] 1 2 [/SUP], Linfen Huang[SUP] 1 2 [/SUP], Stanley Perlman[SUP] 4 [/SUP], Hideki Aihara[SUP] 3 [/SUP], Fang Li[SUP] 1 2 [/SUP]
Affiliations
- PMID: 39083418
- DOI: 10.1073/pnas.2322600121
The animal origin of SARS-CoV-2 remains elusive, lacking a plausible evolutionary narrative that may account for its emergence. Its spike protein resembles certain segments of BANAL-236 and RaTG13, two bat coronaviruses considered possible progenitors of SARS-CoV-2. Additionally, its spike contains a furin motif, a common feature of rodent coronaviruses. To explore the possible involvement of rodents in the emergence of SARS-CoV-2 spike, we examined the crystal structures of the spike receptor-binding domains (RBDs) of BANAL-236 and RaTG13 each complexed with mouse receptor ACE2. Both RBDs have residues at positions 493 and 498 that align well with two virus-binding hotspots on mouse ACE2. Our biochemical evidence supports that both BANAL-236 and RaTG13 spikes can use mouse ACE2 as their entry receptor. These findings point to a scenario in which these bat coronaviruses may have coinfected rodents, leading to a recombination of their spike genes and a subsequent acquisition of a furin motif in rodents, culminating in the emergence of SARS-CoV-2.
Keywords: SARS-CoV-2; X-ray crystallography; angiotensin-converting enzyme 2 (ACE2); receptor-binding domain (RBD); spike protein.