Rhesus angiotensin converting enzyme 2 supports entry of severe acute respiratory syndrome coronavirus in Chinese macaques.
Identifieur interne : 003044 ( Main/Exploration ); précédent : 003043; suivant : 003045Rhesus angiotensin converting enzyme 2 supports entry of severe acute respiratory syndrome coronavirus in Chinese macaques.
Auteurs : Yunxin Chen [République populaire de Chine] ; Li Liu ; Qiang Wei ; Hua Zhu ; Hong Jiang ; Xinming Tu ; Chuan Qin ; Zhiwei ChenSource :
- Virology [ 1096-0341 ] ; 2008.
Descripteurs français
- KwdFr :
- Alignement de séquences, Animaux, Données de séquences moléculaires, Femelle, Humains, Lignée cellulaire, Macaca mulatta (virologie), Mutation, Mâle, Peptidyl-Dipeptidase A (), Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (métabolisme), Poumon (anatomopathologie), Poumon (enzymologie), Poumon (virologie), Pénétration virale, Régulation de l'expression des gènes codant pour des enzymes, Similitude de séquences d'acides aminés, Similitude de séquences d'acides nucléiques, Syndrome respiratoire aigu sévère (anatomopathologie), Syndrome respiratoire aigu sévère (enzymologie), Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Virus du SRAS (physiologie).
- MESH :
- anatomopathologie : Poumon, Syndrome respiratoire aigu sévère.
- enzymologie : Poumon, Syndrome respiratoire aigu sévère.
- génétique : Peptidyl-Dipeptidase A.
- métabolisme : Peptidyl-Dipeptidase A.
- physiologie : Virus du SRAS.
- virologie : Macaca mulatta, Poumon, Syndrome respiratoire aigu sévère.
- Alignement de séquences, Animaux, Données de séquences moléculaires, Femelle, Humains, Lignée cellulaire, Mutation, Mâle, Peptidyl-Dipeptidase A, Pénétration virale, Régulation de l'expression des gènes codant pour des enzymes, Similitude de séquences d'acides aminés, Similitude de séquences d'acides nucléiques, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Line, Female, Gene Expression Regulation, Enzymologic, Humans, Lung (enzymology), Lung (pathology), Lung (virology), Macaca mulatta (virology), Male, Molecular Sequence Data, Mutation, Peptidyl-Dipeptidase A (chemistry), Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (metabolism), SARS Virus (physiology), Sequence Alignment, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Severe Acute Respiratory Syndrome (enzymology), Severe Acute Respiratory Syndrome (pathology), Severe Acute Respiratory Syndrome (virology), Virus Internalization.
- MESH :
- chemical , chemistry : Peptidyl-Dipeptidase A.
- enzymology : Lung, Severe Acute Respiratory Syndrome.
- chemical , genetics : Peptidyl-Dipeptidase A.
- chemical , metabolism : Peptidyl-Dipeptidase A.
- pathology : Lung, Severe Acute Respiratory Syndrome.
- physiology : SARS Virus.
- virology : Lung, Macaca mulatta, Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Animals, Cell Line, Female, Gene Expression Regulation, Enzymologic, Humans, Male, Molecular Sequence Data, Mutation, Sequence Alignment, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Virus Internalization.
Abstract
Angiotensin converting enzyme 2 (ACE2) is the receptor that severe acute respiratory syndrome coronavirus (SARS-CoV) utilizes for target cell entry and, therefore, plays an important role in SARS pathogenesis. Since Chinese rhesus (rh) macaques do not usually develop SARS after SARS-CoV infection, it has been suggested that rh-ACE2 probably does not support viral entry efficiently. To determine the role of rh-ACE2 in early lung pathogenesis in vivo, we studied eleven Chinese rhesus monkeys experimentally infected with a pathogenic SARS-CoV(PUMC01) strain. Rh-ACE2 genes were amplified from all animals by reverse transcription polymerase chain reaction, and their function was studied in vitro using a pseudovirus entry assay. Many natural non-synonymous (NS) changes were found in rh-ACE2 genes. Compared to human (hu) ACE2, thirty-eight consensus NS changes were found in rh-ACE2. Since these changes do not interact with the receptor binding domain of SARS-CoV, rh-ACE2 in general is as effective as human homolog in supporting viral entry. Rh-ACE2, however, is more polymorphic than hu-ACE2. Additional sporadic NS substitutions in clone Rh11-7 reduced the level of rh-ACE2 protein expression and did not support viral entry effectively. Further mutagenesis analysis showed that a natural mutation Y217N dramatically alters ACE2 expression and entry efficiency. Moreover, introduction of the Y217N mutation into hu-ACE2 caused the down-regulation of expression and reduced viral entry efficiency. These results indicate that the Y217N mutation plays a role in modulating SARS-CoV infection. Our results provide insights for understanding the role of rh-ACE2 in SARS lung pathogenesis in a non-human primate model.
DOI: 10.1016/j.virol.2008.08.016
PubMed: 18801550
Affiliations:
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Liu</name></author><author><name sortKey="Wei, Qiang" sort="Wei, Qiang" uniqKey="Wei Q" first="Qiang" last="Wei">Qiang Wei</name></author><author><name sortKey="Zhu, Hua" sort="Zhu, Hua" uniqKey="Zhu H" first="Hua" last="Zhu">Hua Zhu</name></author><author><name sortKey="Jiang, Hong" sort="Jiang, Hong" uniqKey="Jiang H" first="Hong" last="Jiang">Hong Jiang</name></author><author><name sortKey="Tu, Xinming" sort="Tu, Xinming" uniqKey="Tu X" first="Xinming" last="Tu">Xinming Tu</name></author><author><name sortKey="Qin, Chuan" sort="Qin, Chuan" uniqKey="Qin C" first="Chuan" last="Qin">Chuan Qin</name></author><author><name sortKey="Chen, Zhiwei" sort="Chen, Zhiwei" uniqKey="Chen Z" first="Zhiwei" last="Chen">Zhiwei Chen</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18801550</idno><idno type="pmid">18801550</idno><idno type="doi">10.1016/j.virol.2008.08.016</idno><idno 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uniqKey="Chen Y" first="Yunxin" last="Chen">Yunxin Chen</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Laboratory Animal Science, Chinese Academy of Medical Sciences and Peking Union Medical College, No.5, Panjiayuan, Nanli, Chaoyang District, Beijing, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Institute of Laboratory Animal Science, Chinese Academy of Medical Sciences and Peking Union Medical College, No.5, Panjiayuan, Nanli, Chaoyang District, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Liu, Li" sort="Liu, Li" uniqKey="Liu L" first="Li" last="Liu">Li Liu</name></author><author><name sortKey="Wei, Qiang" sort="Wei, Qiang" uniqKey="Wei Q" first="Qiang" last="Wei">Qiang Wei</name></author><author><name sortKey="Zhu, Hua" sort="Zhu, Hua" uniqKey="Zhu H" first="Hua" last="Zhu">Hua Zhu</name></author><author><name sortKey="Jiang, Hong" sort="Jiang, Hong" uniqKey="Jiang H" first="Hong" last="Jiang">Hong Jiang</name></author><author><name sortKey="Tu, Xinming" sort="Tu, Xinming" uniqKey="Tu X" first="Xinming" last="Tu">Xinming Tu</name></author><author><name sortKey="Qin, Chuan" sort="Qin, Chuan" uniqKey="Qin C" first="Chuan" last="Qin">Chuan Qin</name></author><author><name sortKey="Chen, Zhiwei" sort="Chen, Zhiwei" uniqKey="Chen Z" first="Zhiwei" last="Chen">Zhiwei Chen</name></author></analytic><series><title level="j">Virology</title><idno type="eISSN">1096-0341</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Female</term><term>Gene Expression Regulation, Enzymologic</term><term>Humans</term><term>Lung (enzymology)</term><term>Lung (pathology)</term><term>Lung (virology)</term><term>Macaca mulatta (virology)</term><term>Male</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Peptidyl-Dipeptidase A (genetics)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>SARS Virus (physiology)</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Sequence Homology, Nucleic Acid</term><term>Severe Acute Respiratory Syndrome (enzymology)</term><term>Severe Acute Respiratory Syndrome (pathology)</term><term>Severe Acute Respiratory Syndrome (virology)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Données de séquences moléculaires</term><term>Femelle</term><term>Humains</term><term>Lignée cellulaire</term><term>Macaca mulatta (virologie)</term><term>Mutation</term><term>Mâle</term><term>Peptidyl-Dipeptidase A ()</term><term>Peptidyl-Dipeptidase A (génétique)</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Poumon (anatomopathologie)</term><term>Poumon (enzymologie)</term><term>Poumon (virologie)</term><term>Pénétration virale</term><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Similitude de séquences d'acides aminés</term><term>Similitude de séquences d'acides nucléiques</term><term>Syndrome respiratoire aigu sévère (anatomopathologie)</term><term>Syndrome respiratoire aigu sévère (enzymologie)</term><term>Syndrome respiratoire aigu sévère (virologie)</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptidyl-Dipeptidase A</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Poumon</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="enzymologie" 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Virus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Macaca mulatta</term><term>Poumon</term><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Lung</term><term>Macaca mulatta</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Line</term><term>Female</term><term>Gene Expression Regulation, Enzymologic</term><term>Humans</term><term>Male</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term><term>Sequence Homology, Nucleic Acid</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Données de séquences moléculaires</term><term>Femelle</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutation</term><term>Mâle</term><term>Peptidyl-Dipeptidase A</term><term>Pénétration virale</term><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Similitude de séquences d'acides aminés</term><term>Similitude de séquences d'acides nucléiques</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Angiotensin converting enzyme 2 (ACE2) is the receptor that severe acute respiratory syndrome coronavirus (SARS-CoV) utilizes for target cell entry and, therefore, plays an important role in SARS pathogenesis. Since Chinese rhesus (rh) macaques do not usually develop SARS after SARS-CoV infection, it has been suggested that rh-ACE2 probably does not support viral entry efficiently. To determine the role of rh-ACE2 in early lung pathogenesis in vivo, we studied eleven Chinese rhesus monkeys experimentally infected with a pathogenic SARS-CoV(PUMC01) strain. Rh-ACE2 genes were amplified from all animals by reverse transcription polymerase chain reaction, and their function was studied in vitro using a pseudovirus entry assay. Many natural non-synonymous (NS) changes were found in rh-ACE2 genes. Compared to human (hu) ACE2, thirty-eight consensus NS changes were found in rh-ACE2. Since these changes do not interact with the receptor binding domain of SARS-CoV, rh-ACE2 in general is as effective as human homolog in supporting viral entry. Rh-ACE2, however, is more polymorphic than hu-ACE2. Additional sporadic NS substitutions in clone Rh11-7 reduced the level of rh-ACE2 protein expression and did not support viral entry effectively. Further mutagenesis analysis showed that a natural mutation Y217N dramatically alters ACE2 expression and entry efficiency. Moreover, introduction of the Y217N mutation into hu-ACE2 caused the down-regulation of expression and reduced viral entry efficiency. These results indicate that the Y217N mutation plays a role in modulating SARS-CoV infection. Our results provide insights for understanding the role of rh-ACE2 in SARS lung pathogenesis in a non-human primate model.</div></front></TEI><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Chen, Zhiwei" sort="Chen, Zhiwei" uniqKey="Chen Z" first="Zhiwei" last="Chen">Zhiwei Chen</name><name sortKey="Jiang, Hong" sort="Jiang, Hong" uniqKey="Jiang H" first="Hong" last="Jiang">Hong Jiang</name><name sortKey="Liu, Li" sort="Liu, Li" uniqKey="Liu L" first="Li" last="Liu">Li Liu</name><name sortKey="Qin, Chuan" sort="Qin, Chuan" uniqKey="Qin C" first="Chuan" last="Qin">Chuan Qin</name><name sortKey="Tu, Xinming" sort="Tu, Xinming" uniqKey="Tu X" first="Xinming" last="Tu">Xinming Tu</name><name sortKey="Wei, Qiang" sort="Wei, Qiang" uniqKey="Wei Q" first="Qiang" last="Wei">Qiang Wei</name><name sortKey="Zhu, Hua" sort="Zhu, Hua" uniqKey="Zhu H" first="Hua" last="Zhu">Hua Zhu</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Chen, Yunxin" sort="Chen, Yunxin" uniqKey="Chen Y" first="Yunxin" last="Chen">Yunxin Chen</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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