ArticleCell2021
Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species.
Article in Cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.
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Who cites it
100 citing papers in PubMed, 154 citations in OpenAlex.
- T-cell receptor repertoires as potential diagnostic markers for patients with COVID-19.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2021Trial
- New visual culture of science: analysis of graphical abstracts in the life science journal "Cell".History and philosophy of the life sciences · 2026Article
- Structural dynamics and allosteric communication of a SARS-like bat coronavirus spike glycoprotein.Biophysical journal · 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
- Development of a Thermostable and Broadly Neutralizing Pan-Sarbecovirus Vaccine Candidate.ACS infectious diseases · 2026Article
- Development of the coronavirus reverse genetic system: Core technology for pathogenesis mechanisms research and vaccine/drug development.Virulence · 2025Review
- Critical amino acid residues in human ACE2 for SARS-CoV-2 spike protein binding and virus entry.Microbiology spectrum · 2025Article
- Synergistic activation of bat SARS-like coronaviruses spike protein by elastase and TMPRSS2.Scientific reports · 2025Article
- Genetic diversity of sarbecoviruses isolated from microbats in Southern Japan.Virology journal · 2025Article
- Molecular mechanisms of RaTG13 and SARS-CoV-2 RBD bound to Rhinolophus affinis bat ACE2.Protein science : a publication of the Protein Society · 2025Article
- Structural basis and mode of action for two broadly neutralizing nanobodies targeting the highly conserved spike stem-helix of sarbecoviruses including SARS-CoV-2 and its variants.PLoS pathogens · 2025Article
- Article
- SARS-related coronavirus S-protein structures reveal synergistic RBM interactions underpinning high-affinity human ACE2 binding.Science advances · 2025Article
- Rapid preparation and characterization of pan-sarbecovirus mRNA vaccine candidates based on the receptor binding domain.Virologica Sinica · 2025Article
- The Batalogue: an overview of betacoronaviruses with future pandemic potential.FEMS microbiology reviews · 2025Review
- Cross-species recognition of two porcine coronaviruses to their cellular receptor aminopeptidase N of dogs and seven other species.PLoS pathogens · 2025Article
- Predictive multi-omic biomarkers for urban zoonotic spillover detection: an integrative review.Frontiers in public health · 2025Review
- Interfacial subregions of SARS-CoV-2 spike RBD to hACE2 affect intermolecular affinity by their distinct roles played in association and dissociation kinetics.Communications biology · 2024Article
- Cellular sialoglycans are differentially required for endosomal and cell-surface entry of SARS-CoV-2 in lung cell lines.PLoS pathogens · 2024Article
40 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
24 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been spreading worldwide, causing a global pandemic. Bat-origin RaTG13 is currently the most phylogenetically related virus. Here we obtained the complex structure of the RaTG13 receptor binding domain (RBD) with human ACE2 (hACE2) and evaluated binding of RaTG13 RBD to 24 additional ACE2 orthologs. By substituting residues in the RaTG13 RBD with their counterparts in the SARS-CoV-2 RBD, we found that residue 501, the major position found in variants of concern (VOCs) 501Y.V1/V2/V3, plays a key role in determining the potential host range of RaTG13. We also found that SARS-CoV-2 could induce strong cross-reactive antibodies to RaTG13 and identified a SARS-CoV-2 monoclonal antibody (mAb), CB6, that could cross-neutralize RaTG13 pseudovirus. These results elucidate the receptor binding and host adaption mechanisms of RaTG13 and emphasize the importance of continuous surveillance of coronaviruses (CoVs) carried by animal reservoirs to prevent another spillover of 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.