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 : 001729 ( PubMed/Curation ); précédent : 001728; suivant : 001730Identification 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 WangSource :
- The Journal of general virology [ 1465-2099 ] ; 2010.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Peptidyl-Dipeptidase A.
- métabolisme : Peptidyl-Dipeptidase A.
- physiologie : Virus du SRAS.
- Animaux, Chiroptera, Données de séquences moléculaires, Peptidyl-Dipeptidase A, Pénétration virale, Récepteurs de surface cellulaire, Spécificité d'espèce, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Peptidyl-Dipeptidase A.
- chemical , genetics : Peptidyl-Dipeptidase A.
- chemical , metabolism : Peptidyl-Dipeptidase A.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Chiroptera, Molecular Sequence Data, Receptors, Cell Surface, Species Specificity, Virus Internalization.
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
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pubmed:20335495Le document en format XML
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Crameri</name></author><author><name sortKey="Shi, Zhengli" sort="Shi, Zhengli" uniqKey="Shi Z" first="Zhengli" last="Shi">Zhengli Shi</name></author><author><name sortKey="Wang, Lin Fa" sort="Wang, Lin Fa" uniqKey="Wang L" first="Lin-Fa" last="Wang">Lin-Fa Wang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20335495</idno><idno type="pmid">20335495</idno><idno type="doi">10.1099/vir.0.020172-0</idno><idno type="wicri:Area/PubMed/Corpus">001729</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001729</idno><idno type="wicri:Area/PubMed/Curation">001729</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001729</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification of key amino acid residues required for horseshoe bat angiotensin-I converting enzyme 2 to function as a receptor for 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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. 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