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 : 002100 ( Ncbi/Merge ); précédent : 002099; suivant : 002101Identification 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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- to stream PubMed, to step Corpus: 001729
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pubmed:20335495Le document en format XML
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<term>Peptidyl-Dipeptidase A (genetics)</term>
<term>Peptidyl-Dipeptidase A (metabolism)</term>
<term>Receptors, Cell Surface</term>
<term>SARS Virus (physiology)</term>
<term>Species Specificity</term>
<term>Virus Internalization</term>
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<term>Peptidyl-Dipeptidase A (génétique)</term>
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<term>Récepteurs de surface cellulaire</term>
<term>Spécificité d'espèce</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS (physiologie)</term>
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<term>Données de séquences moléculaires</term>
<term>Peptidyl-Dipeptidase A</term>
<term>Pénétration virale</term>
<term>Récepteurs de surface cellulaire</term>
<term>Spécificité d'espèce</term>
<term>Séquence d'acides aminés</term>
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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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