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
Identifieur interne : 002935 ( Main/Exploration ); précédent : 002934; suivant : 002936Identification 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
Auteurs : MENG YU [Australie] ; Mary Tachedjian [Australie] ; Gary Crameri [Australie] ; ZHENGLI SHI [République populaire de Chine] ; Lin-Fa Wang [Australie]Source :
- Journal of general virology [ 0022-1317 ] ; 2010.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Enzyme.
English descriptors
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.
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PascalFrancis, to step Corpus: 000138
- to stream PascalFrancis, to step Curation: 000850
- to stream PascalFrancis, to step Checkpoint: 000144
- to stream Main, to step Merge: 002976
- to stream Main, to step Curation: 002935
Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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