Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus

UMMS Affiliation

Department of Pediatrics; Program in Molecular Medicine



Document Type


Medical Subject Headings

Animals; Antibodies; Carboxypeptidases; Cell Line; Cercopithecus aethiops; Giant Cells; Humans; Membrane Glycoproteins; Molecular Weight; Peptidyl-Dipeptidase A; Protein Binding; Protein Structure, Tertiary; Receptors, Virus; SARS Virus; Solubility; Transfection; Vero Cells; Viral Envelope Proteins; Virus Replication


Immunology and Infectious Disease | Pediatrics


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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Citation: Nature. 2003 Nov 27;426(6965):450-4. Link to article on publisher's site

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