Angiotensin-converting enzyme 2 (ACE2) proteins of different bat species confer variable susceptibility to SARS-CoV entry
Identifieur interne : 002881 ( Main/Exploration ); précédent : 002880; suivant : 002882Angiotensin-converting enzyme 2 (ACE2) proteins of different bat species confer variable susceptibility to SARS-CoV entry
Auteurs : Yuxuan Hou [République populaire de Chine] ; Cheng Peng [République populaire de Chine] ; Meng Yu [Australie] ; Yan Li [République populaire de Chine] ; Zhenggang Han [République populaire de Chine] ; Fang Li [États-Unis] ; Lin-Fa Wang [Australie] ; Zhengli Shi [République populaire de Chine]Source :
- Archives of Virology [ 0304-8608 ] ; 2010-10-01.
Descripteurs français
- KwdFr :
- ARN viral (génétique), Alignement de séquences, Analyse de séquence d'ADN, Animaux, Cellules HeLa, Chiroptera, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Liaison aux protéines, Modèles moléculaires, Mutagenèse dirigée, Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (métabolisme), Peptidyl-Dipeptidase A (physiologie), Protéines de l'enveloppe virale (métabolisme), Protéines mutantes (génétique), Protéines mutantes (métabolisme), Pénétration virale, Récepteurs viraux (génétique), Récepteurs viraux (métabolisme), Récepteurs viraux (physiologie), Réservoirs d'agents pathogènes, Structure tertiaire des protéines, Substitution d'acide aminé, Séquence d'acides aminés, Variation génétique, Virus du SRAS (physiologie).
- MESH :
- génétique : ARN viral, Peptidyl-Dipeptidase A, Protéines mutantes, Récepteurs viraux.
- métabolisme : Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Protéines mutantes, Récepteurs viraux.
- physiologie : Peptidyl-Dipeptidase A, Récepteurs viraux, Virus du SRAS.
- Alignement de séquences, Analyse de séquence d'ADN, Animaux, Cellules HeLa, Chiroptera, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Humains, Liaison aux protéines, Modèles moléculaires, Mutagenèse dirigée, Pénétration virale, Réservoirs d'agents pathogènes, Structure tertiaire des protéines, Substitution d'acide aminé, Séquence d'acides aminés, Variation génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Animals, Chiroptera, Disease Reservoirs, Genetic Variation, HeLa Cells, Humans, Membrane Glycoproteins (metabolism), Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutant Proteins (genetics), Mutant Proteins (metabolism), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (metabolism), Peptidyl-Dipeptidase A (physiology), Protein Binding, Protein Structure, Tertiary, RNA, Viral (genetics), Receptors, Virus (genetics), Receptors, Virus (metabolism), Receptors, Virus (physiology), SARS Virus (physiology), Sequence Alignment, Sequence Analysis, DNA, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), Virus Internalization.
- MESH :
- chemical , genetics : Mutant Proteins, Peptidyl-Dipeptidase A, RNA, Viral, Receptors, Virus.
- chemical , metabolism : Membrane Glycoproteins, Mutant Proteins, Peptidyl-Dipeptidase A, Receptors, Virus, Viral Envelope Proteins.
- chemical , physiology : Peptidyl-Dipeptidase A, Receptors, Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Chiroptera, Disease Reservoirs, Genetic Variation, HeLa Cells, Humans, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Sequence Analysis, DNA, Spike Glycoprotein, Coronavirus, Virus Internalization.
Abstract
Abstract: The discovery of SARS-like coronavirus in bats suggests that bats could be the natural reservoir of SARS-CoV. However, previous studies indicated the angiotensin-converting enzyme 2 (ACE2) protein, a known SARS-CoV receptor, from a horseshoe bat was unable to act as a functional receptor for SARS-CoV. Here, we extended our previous study to ACE2 molecules from seven additional bat species and tested their interactions with human SARS-CoV spike protein using both HIV-based pseudotype and live SARS-CoV infection assays. The results show that ACE2s of Myotis daubentoni and Rhinolophus sinicus support viral entry mediated by the SARS-CoV S protein, albeit with different efficiency in comparison to that of the human ACE2. Further, the alteration of several key residues either decreased or enhanced bat ACE2 receptor efficiency, as predicted from a structural modeling study of the different bat ACE2 molecules. These data suggest that M. daubentoni and R. sinicus are likely to be susceptible to SARS-CoV and may be candidates as the natural host of the SARS-CoV progenitor viruses. Furthermore, our current study also demonstrates that the genetic diversity of ACE2 among bats is greater than that observed among known SARS-CoV susceptible mammals, highlighting the possibility that there are many more uncharacterized bat species that can act as a reservoir of SARS-CoV or its progenitor viruses. This calls for continuation and expansion of field surveillance studies among different bat populations to eventually identify the true natural reservoir of SARS-CoV.
Url:
- https://api.istex.fr/ark:/67375/VQC-BBLB78R6-D/fulltext.pdf
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7086629
DOI: 10.1007/s00705-010-0729-6
Affiliations:
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Le document en format XML
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Molecular</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Sequence Analysis, DNA</term><term>Spike Glycoprotein, Coronavirus</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Analyse de séquence d'ADN</term><term>Animaux</term><term>Cellules HeLa</term><term>Chiroptera</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Mutagenèse dirigée</term><term>Pénétration virale</term><term>Réservoirs d'agents pathogènes</term><term>Structure tertiaire des protéines</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term><term>Variation génétique</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The discovery of SARS-like coronavirus in bats suggests that bats could be the natural reservoir of SARS-CoV. However, previous studies indicated the angiotensin-converting enzyme 2 (ACE2) protein, a known SARS-CoV receptor, from a horseshoe bat was unable to act as a functional receptor for SARS-CoV. Here, we extended our previous study to ACE2 molecules from seven additional bat species and tested their interactions with human SARS-CoV spike protein using both HIV-based pseudotype and live SARS-CoV infection assays. The results show that ACE2s of Myotis daubentoni and Rhinolophus sinicus support viral entry mediated by the SARS-CoV S protein, albeit with different efficiency in comparison to that of the human ACE2. Further, the alteration of several key residues either decreased or enhanced bat ACE2 receptor efficiency, as predicted from a structural modeling study of the different bat ACE2 molecules. These data suggest that M. daubentoni and R. sinicus are likely to be susceptible to SARS-CoV and may be candidates as the natural host of the SARS-CoV progenitor viruses. Furthermore, our current study also demonstrates that the genetic diversity of ACE2 among bats is greater than that observed among known SARS-CoV susceptible mammals, highlighting the possibility that there are many more uncharacterized bat species that can act as a reservoir of SARS-CoV or its progenitor viruses. This calls for continuation and expansion of field surveillance studies among different bat populations to eventually identify the true natural reservoir of SARS-CoV.</div></front></TEI><affiliations><list><country><li>Australie</li><li>République populaire de Chine</li><li>États-Unis</li></country><region><li>Minnesota</li></region></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Hou, Yuxuan" sort="Hou, Yuxuan" uniqKey="Hou Y" first="Yuxuan" last="Hou">Yuxuan Hou</name></noRegion><name sortKey="Han, Zhenggang" sort="Han, Zhenggang" uniqKey="Han Z" first="Zhenggang" last="Han">Zhenggang Han</name><name sortKey="Li, Yan" sort="Li, Yan" uniqKey="Li Y" first="Yan" last="Li">Yan Li</name><name sortKey="Peng, Cheng" sort="Peng, Cheng" uniqKey="Peng C" first="Cheng" last="Peng">Cheng Peng</name><name sortKey="Shi, Zhengli" sort="Shi, Zhengli" uniqKey="Shi Z" first="Zhengli" last="Shi">Zhengli Shi</name><name sortKey="Shi, Zhengli" sort="Shi, Zhengli" uniqKey="Shi Z" first="Zhengli" last="Shi">Zhengli Shi</name></country><country name="Australie"><noRegion><name sortKey="Yu, Meng" sort="Yu, Meng" uniqKey="Yu M" first="Meng" last="Yu">Meng Yu</name></noRegion><name sortKey="Wang, Lin Fa" sort="Wang, Lin Fa" uniqKey="Wang L" first="Lin-Fa" last="Wang">Lin-Fa Wang</name><name sortKey="Wang, Lin Fa" sort="Wang, Lin Fa" uniqKey="Wang L" first="Lin-Fa" last="Wang">Lin-Fa Wang</name></country><country name="États-Unis"><region name="Minnesota"><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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