8UZF

Crystal structure of chimeric RaTG13 RBD complexed with chimeric mouse ACE2

Summary for 8UZF

• Entry DOI: 10.2210/pdb8uzf/pdb
• Descriptor: Angiotensin-converting enzyme 2, Receptor binding domain, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: rbd, ace2, viral protein-hydrolase complex, viral protein, viral protein/hydrolase
• Biological source: Mus musculus (mouse); More
• Total number of polymer chains: 4
• Total formula weight: 189631.35

Authors

Zhang, W.,Shi, K.,Aihara, H.,Li, F. (deposition date: 2023-11-15, release date: 2024-07-24, Last modification date: 2025-02-05)

Primary citation

Zhang, W.,Shi, K.,Hsueh, F.C.,Mendoza, A.,Ye, G.,Huang, L.,Perlman, S.,Aihara, H.,Li, F.
Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses.
Proc.Natl.Acad.Sci.USA, 121:e2322600121-e2322600121, 2024

PubMed Abstract: 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.

PubMed: 39083418
DOI: 10.1073/pnas.2322600121

Experimental method

X-RAY DIFFRACTION (3.283 Å)