ArticlePLoS biology2022
Expanded ACE2 dependencies of diverse SARS-like coronavirus receptor binding domains.
Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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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Who cites it
37 citing papers in PubMed, 48 citations in OpenAlex.
- Article
- Breadth of ACE2 receptor usage predicts host range and antigenic relatedness across bat sarbecoviruses.PLoS biology · 2026Article
- Targeting of conserved spike epitopes enables broad antibody neutralisation of diverse bat sarbecoviruses.PLoS biology · 2026Article
- Kozak sequence libraries for systematically characterizing transgenes across expression levels.Nucleic acids research · 2026Article
- Exploring coronavirus cell entry with functional viromics.Journal of virology · 2026Review
- Article
- Development of a Thermostable and Broadly Neutralizing Pan-Sarbecovirus Vaccine Candidate.ACS infectious diseases · 2026Article
- Severity-associated cross-reactive anti-sarbecovirus antibody responses in COVID-19 convalescents and isolation of a dual-targeting monoclonal antibody with cross-neutralizing activity.Frontiers in immunology · 2026Article
- Experimental evolution of Rc-o319 sarbecovirus spike protein reveals limited ACE2 adaptability.Virus evolution · 2026Article
- Rapid Discovery of Potent Neutralizing Antibodies against SARS-CoV-2 through Directed Evolution of SARS-CoV-1 Antibodies.Molecular pharmaceutics · 2025Article
- Identification and characterization of novel bat coronaviruses in Spain.PLoS pathogens · 2025Article
- Design of SARS-CoV-2 RBD immunogens to focus immune responses toward conserved coronavirus epitopes.Journal of virology · 2025Article
- Synergistic activation of bat SARS-like coronaviruses spike protein by elastase and TMPRSS2.Scientific reports · 2025Article
- ACE2 from Pipistrellus abramus bats is a receptor for HKU5 coronaviruses.Nature communications · 2025Article
- SARS-related coronavirus S-protein structures reveal synergistic RBM interactions underpinning high-affinity human ACE2 binding.Science advances · 2025Article
- Bioinformatic Tools for Studying the Cellular Immune Response to SARS-CoV-2, Vaccine Efficacy, and Future Pandemics at the Global Population Level.International journal of molecular sciences · 2024Review
- ACE2-independent sarbecovirus cell entry can be supported by TMPRSS2-related enzymes and can reduce sensitivity to antibody-mediated neutralization.PLoS pathogens · 2024Article
- Sarbecovirus RBD indels and specific residues dictating multi-species ACE2 adaptiveness.Nature communications · 2024Article
- Delineating the functional activity of antibodies with cross-reactivity to SARS-CoV-2, SARS-CoV-1 and related sarbecoviruses.PLoS pathogens · 2024Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Viral spillover from animal reservoirs can trigger public health crises and cripple the world economy. Knowing which viruses are primed for zoonotic transmission can focus surveillance efforts and mitigation strategies for future pandemics. Successful engagement of receptor protein orthologs is necessary during cross-species transmission. The clade 1 sarbecoviruses including Severe Acute Respiratory Syndrome-related Coronavirus (SARS-CoV) and SARS-CoV-2 enter cells via engagement of angiotensin converting enzyme-2 (ACE2), while the receptor for clade 2 and clade 3 remains largely uncharacterized. We developed a mixed cell pseudotyped virus infection assay to determine whether various clades 2 and 3 sarbecovirus spike proteins can enter HEK 293T cells expressing human or Rhinolophus horseshoe bat ACE2 proteins. The receptor binding domains from BtKY72 and Khosta-2 used human ACE2 for entry, while BtKY72 and Khosta-1 exhibited widespread use of diverse rhinolophid ACE2s. A lysine at ACE2 position 31 appeared to be a major determinant of the inability of these RBDs to use a certain ACE2 sequence. The ACE2 protein from Rhinolophus alcyone engaged all known clade 3 and clade 1 receptor binding domains. We observed little use of Rhinolophus ACE2 orthologs by the clade 2 viruses, supporting the likely use of a separate, unknown receptor. Our results suggest that clade 3 sarbecoviruses from Africa and Europe use Rhinolophus ACE2 for entry, and their spike proteins appear primed to contribute to zoonosis under the right conditions.
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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.