ArticleProceedings of the National Academy of Sciences of the United States of America2024
Structural basis for mouse receptor recognition by bat SARS2-like coronaviruses.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Epidemiological surveillance and genomic characterisation of betacoronavirus inOne health (Amsterdam, Netherlands) · 2026Article
- Article
- Update and reuse: Structure-guided nanobody evolution against SARS-CoV-2 escape.PLoS pathogens · 2026Article
- Structural basis for bat receptor recognition by SARS-CoV-2 and bat SARS2-like coronaviruses.Communications biology · 2026Article
- Structural and functional constraints on spike activation and host protease utilization limit cell entry of SARS-CoV-2-related bat coronaviruses.Journal of virology · 2025Article
- Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1.Communications biology · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
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.
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Registered trials
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