@article{mbs:/content/journal/jgv/10.1099/vir.0.020172-0, author = "Yu, Meng and Tachedjian, Mary and Crameri, Gary and Shi, Zhengli and Wang, Lin-Fa", title = "Identification of key amino acid residues required for horseshoe bat angiotensin-I converting enzyme 2 to function as a receptor for severe acute respiratory syndrome coronavirus", journal= "Journal of General Virology", year = "2010", volume = "91", number = "7", pages = "1708-1712", doi = "https://doi.org/10.1099/vir.0.020172-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.020172-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "Angiotensin-I converting enzyme 2 (ACE2) is the receptor for severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV). A previous study indicated that ACE2 from a horseshoe bat, the host of a highly related SARS-like coronavirus, could not function as a receptor for SARS-CoV. Here, we demonstrate that a 3 aa change from SHE (aa 40–42) to FYQ was sufficient to convert the bat ACE2 into a fully functional receptor for SARS-CoV. We further demonstrate that an ACE2 molecule from a fruit bat, which contains the FYQ motif, was able to support SARS-CoV infection, indicating a potentially much wider host range for SARS-CoV-related viruses among different bat populations.", }