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Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Open accessAbstract
Spike (S) proteins of coronaviruses, including the coronavirus that causes severe acute respiratory syndrome (SARS), associate with cellular receptors to mediate infection of their target cells. Here we identify a metallopeptidase, angiotensin-converting enzyme 2 (ACE2), isolated from SARS coronavirus (SARS-CoV)-permissive Vero E6 cells, that efficiently binds the S1 domain of the SARS-CoV S protein. We found that a soluble form of ACE2, but not of the related enzyme ACE1, blocked association of the S1 domain with Vero E6 cells. 293T cells transfected with ACE2, but not those transfected with human immunodeficiency virus-1 receptors, formed multinucleated syncytia with cells expressing S protein. Furthermore, SARS-CoV replicated efficiently on ACE2-transfected but not mock-transfected 293T cells. Finally, anti-ACE2 but not anti-ACE1 antibody blocked viral replication on Vero E6 cells. Together our data indicate that ACE2 is a functional receptor for SARS-CoV.
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“Importantly, ACE2 (angiotensin-converting enzyme 2) had been identified as the receptor for SARS-CoV 4,5 and SARS-CoV-2.”
From COVID-19, Myocarditis and Pericarditis (2023) · cites this paper as [5]
In the citing paper
“Study of Zhou et al.4 indicated that the angiotensin-converting enzyme II (ACE2) is likely the cell receptor of 2019-nCoV, which were also the receptor for SARS-CoV and HCoV-NL637,8.”
From High expression of ACE2 receptor of 2019-nCoV on the epithelial cells of oral mucosa (2020) · cites this paper as [7]
In the citing paper
“The cell surface receptor for the CoV-1 and CoV-2 surface spike protein has been identified by affinity-MS to be angiotensin-converting enzyme 2 (ACE2)147”
From A high-stringency blueprint of the human proteome (2020) · cites this paper as [147]
In the citing paper
“As an alternative approach, cellular interaction partners for a single viral protein of interest have also been investigated by in vitro incubation of the viral protein bait with lysates from uninfected permissive cells.”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [59]
In the citing paper
“while promoted upon ACE2 overexpression in HEK293T cells that are otherwise non-permissive to SARS-CoV.”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [59]
In the citing paper
“which was further functionally characterized as a functional receptor for SARS-CoV.”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [59]
In the citing paper
“MS analysis revealed the cellular metallopeptidase angiotensin-converting enzyme 2 (ACE2) as an S1 interaction partner”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [59]
In the citing paper
“Viral replication was inhibited upon incubation with antibodies against ACE2”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [59]
In the citing paper
“This interaction requires cleavage of the S protein, likely by the cell surface protease TMPRSS2, although other proteases (such as Cathepsin B and L, CTSB/CTSL) may also be involved (4-6, 22-25).”
From Non-neuronal expression of SARS-CoV-2 entry genes in the olfactory system suggests mechanisms underlying COVID-19-associated anosmia (2020) · cites this paper as [23]
In the citing paper
“CoV-2 — like SARS-CoV — infects cells through interactions between its spike (S) protein and the ACE2 protein on target cells.”
From Non-neuronal expression of SARS-CoV-2 entry genes in the olfactory system suggests mechanisms underlying COVID-19-associated anosmia (2020) · cites this paper as [23]
In the citing paper
“ACE2 is the functional entry receptor for both severe acute respiratory syndrome (SARS) coronaviruses, SARS-CoV (36) and SARS-CoV-2 (37).”
From TCRD and pharos 2021: mining the human proteome for disease biology (2021) · cites this paper as [36]
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Metadata
- Authors
- Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., Choe, H., & Farzan, M.
- Affiliations
- Brigham and Women's Hospital (US)
- Harvard University (US)
- Tufts University (US)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Choe, Hyeryun
- Farzan, Michael
- ORCID
- Venue
- Nature
- Published
- 2003-11-27
- Volume
- 426
- Issue
- 6965
- Pages
- 450-454
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7095016
- OpenAlex
- W1966238900
- Cited by
- 5,923
- References
- 32
- Citations by year
- 2026: 74 · 2025: 145 · 2024: 298 · 2023: 448 · 2022: 732 · 2021: 1288 · 2020: 1794 · 2019: 32 · 2018: 30 · 2017: 44 · 2016: 50 · 2015: 49 · 2014: 62 · 2013: 43 · 2012: 50
- FWCI
- 79.30
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Science Foundation
- National Aeronautics and Space Administration
- Hawaii Community Foundation
- Topics
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Keywords
- angiotensin-converting enzyme 2, SARS coronavirus, viral receptor, receptor binding, syncytium formation, viral replication, ACE1, Vero E6 cells, HEK293T cells, antibody inhibition
- MeSH terms
- Angiotensin-Converting Enzyme 2, Animals, Antibodies, Carboxypeptidases, Cell Line, Chlorocebus aethiops, Humans, Peptidyl-Dipeptidase A, Membrane Glycoproteins, Molecular Weight, Protein Binding, Receptors, Virus, Solubility, Transfection, Vero Cells, Viral Envelope Proteins, Virus Replication, Giant Cells, Protein Structure, Tertiary, Severe acute respiratory syndrome-related coronavirus, Spike Glycoprotein, Coronavirus
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