Li, WenhuiGreenough, Thomas C.Moore, Michael J.Vasilieva, NatalyaSomasundaran, MohanSullivan, John L.Farzan, MichaelChoe, Hyeryun2022-08-232022-08-232004-10-012012-05-01J Virol. 2004 Oct;78(20):11429-33. <a href="http://dx.doi.org/10.1128/JVI.78.20.11429-11433.2004">Link to article on publisher's site</a>0022-538X (Linking)10.1128/JVI.78.20.11429-11433.200415452268https://hdl.handle.net/20.500.14038/43459Replication of viruses in species other than their natural hosts is frequently limited by entry and postentry barriers. The coronavirus that causes severe acute respiratory syndrome (SARS-CoV) utilizes the receptor angiotensin-converting enzyme 2 (ACE2) to infect cells. Here we compare human, mouse, and rat ACE2 molecules for their ability to serve as receptors for SARS-CoV. We found that, compared to human ACE2, murine ACE2 less efficiently bound the S1 domain of SARS-CoV and supported less-efficient S protein-mediated infection. Rat ACE2 was even less efficient, at near background levels for both activities. Murine 3T3 cells expressing human ACE2 supported SARS-CoV replication, whereas replication was less than 10% as efficient in the same cells expressing murine ACE2. These data imply that a mouse transgenically expressing human ACE2 may be a useful animal model of SARS.en-US3T3 CellsAnimalsCell LineEndopeptidasesHumansMicePeptidyl-Dipeptidase ARatsSARS VirusSevere Acute Respiratory Syndrome*Virus ReplicationImmunology and Infectious DiseasePediatricsJournal Articlehttps://escholarship.umassmed.edu/peds_immunology/412814371peds_immunology/41