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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 : 002526 ( Main/Exploration ); précédent : 002525; suivant : 002527

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.

Auteurs : Meng Yu [Australie] ; Mary Tachedjian ; Gary Crameri ; Zhengli Shi ; Lin-Fa Wang

Source :

RBID : pubmed:20335495

Descripteurs français

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.

DOI: 10.1099/vir.0.020172-0
PubMed: 20335495


Affiliations:


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