ArticleThe EMBO journal2021
Molecular basis of cross-species ACE2 interactions with SARS-CoV-2-like viruses of pangolin origin.
Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 55 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
55 citing papers in PubMed, 69 citations in OpenAlex.
- Pangolin-Associated Viruses: Diversity, Evolutionary Adaptation, and Zoonotic Spillover Risks.Animals : an open access journal from MDPI · 2026Review
- Structure and receptor recognition of type-II feline infectious peritonitis virus spike glycoprotein.The EMBO journal · 2026Article
- Genetic diversity of pangolin coronaviruses reveals a key immuno-evasive substitution at spike residue 519.Journal of virology · 2026Article
- COVID-19 vaccination induces cross-neutralisation of sarbecoviruses related to SARS-CoV-2.NPJ vaccines · 2026Article
- RAISE: A computational tool for evaluating sarbecovirus spillover potential.Nature communications · 2026Article
- Molecular basis of fox ACE2 recognition by receptor binding domains of SARS-CoV-2 and PCoV-GD.Cell insight · 2026Article
- Receptor affinity-selective differential dynamics of membrane fusion initiation govern deltacoronavirus cross-species transmission.Science China. Life sciences · 2025Article
- CX1/BtSY2 and BANAL-20-52 exhibit broader receptor binding and higher affinities to multiple animal ACE2 orthologs than SARS-CoV-2 prototype.Journal of virology · 2025Article
- Rapid and accurate detection of infectious SARS-CoV-2 by viral receptor capture combined with loop-mediated isothermal amplification.Virologica Sinica · 2025Article
- Receptor Binding for the Entry Mechanisms of SARS-CoV-2: Insights from the Original Strain and Emerging Variants.Viruses · 2025Review
- Molecular mechanisms of RaTG13 and SARS-CoV-2 RBD bound to Rhinolophus affinis bat ACE2.Protein science : a publication of the Protein Society · 2025Article
- Cross-species recognition of two porcine coronaviruses to their cellular receptor aminopeptidase N of dogs and seven other species.PLoS pathogens · 2025Article
- Sarbecovirus RBD indels and specific residues dictating multi-species ACE2 adaptiveness.Nature communications · 2024Article
- Article
- Self-assembled superstructure alleviates air-water interface effect in cryo-EM.Nature communications · 2024Article
- Characterization of a pangolin SARS-CoV-2-related virus isolate that uses the human ACE2 receptor.Science China. Life sciences · 2024Article
- Article
- Neutralizing antibodies reveal cryptic vulnerabilities and interdomain crosstalk in the porcine deltacoronavirus spike protein.Nature communications · 2024Article
- Structural basis and analysis of hamster ACE2 binding to different SARS-CoV-2 spike RBDs.Journal of virology · 2024Article
- Emergence of SARS and COVID-19 and preparedness for the next emerging disease X.Frontiers of medicine · 2024Review
Corrections and comments
- Erratum issued
Authors and funding
16 authors at 5 institutions in 2 countries.
Funding
Abstract
Pangolins have been suggested as potential reservoir of zoonotic viruses, including SARS-CoV-2 causing the global COVID-19 outbreak. Here, we study the binding of two SARS-CoV-2-like viruses isolated from pangolins, GX/P2V/2017 and GD/1/2019, to human angiotensin-converting enzyme 2 (hACE2), the receptor of SARS-CoV-2. We find that the spike protein receptor-binding domain (RBD) of pangolin CoVs binds to hACE2 as efficiently as the SARS-CoV-2 RBD in vitro. Furthermore, incorporation of pangolin CoV RBDs allows entry of pseudotyped VSV particles into hACE2-expressing cells. A screen for binding of pangolin CoV RBDs to ACE2 orthologs from various species suggests a broader host range than that of SARS-CoV-2. Additionally, cryo-EM structures of GX/P2V/2017 and GD/1/2019 RBDs in complex with hACE2 show their molecular binding in modes similar to SARS-CoV-2 RBD. Introducing the Q498H substitution found in pangolin CoVs into the SARS-CoV-2 RBD expands its binding capacity to ACE2 homologs of mouse, rat, and European hedgehog. These findings suggest that these two pangolin CoVs may infect humans, highlighting the necessity of further surveillance of pangolin CoVs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.