Modulation of TNF-alpha-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-alpha production and facilitates viral entry.
Identifieur interne : 003075 ( Main/Exploration ); précédent : 003074; suivant : 003076Modulation of TNF-alpha-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-alpha production and facilitates viral entry.
Auteurs : Shiori Haga [Japon] ; Norio Yamamoto ; Chikako Nakai-Murakami ; Yoshiaki Osawa ; Kenzo Tokunaga ; Tetsutaro Sata ; Naoki Yamamoto ; Takehiko Sasazuki ; Yukihito IshizakaSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2008.
Descripteurs français
- KwdFr :
- ARN messager (métabolisme), Animaux, Délétion de séquence, Facteur de nécrose tumorale alpha (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Lignée cellulaire, Peptidyl-Dipeptidase A (génétique), Peptidyl-Dipeptidase A (métabolisme), Petit ARN interférent (génétique), Protéine ADAM17, Protéines ADAM (métabolisme), Protéines de l'enveloppe virale (métabolisme), Pénétration virale, Souris, Structure tertiaire des protéines (génétique), Virus du SRAS (génétique), Virus du SRAS (physiologie).
- MESH :
- génétique : Peptidyl-Dipeptidase A, Petit ARN interférent, Structure tertiaire des protéines, Virus du SRAS.
- métabolisme : ARN messager, Facteur de nécrose tumorale alpha, Glycoprotéines membranaires, Peptidyl-Dipeptidase A, Protéines ADAM, Protéines de l'enveloppe virale.
- physiologie : Virus du SRAS.
- Animaux, Délétion de séquence, Glycoprotéine de spicule des coronavirus, Humains, Lignée cellulaire, Protéine ADAM17, Pénétration virale, Souris.
English descriptors
- KwdEn :
- ADAM Proteins (metabolism), ADAM17 Protein, Animals, Cell Line, Humans, Membrane Glycoproteins (metabolism), Mice, Peptidyl-Dipeptidase A (genetics), Peptidyl-Dipeptidase A (metabolism), Protein Structure, Tertiary (genetics), RNA, Messenger (metabolism), RNA, Small Interfering (genetics), SARS Virus (genetics), SARS Virus (physiology), Sequence Deletion, Spike Glycoprotein, Coronavirus, Tumor Necrosis Factor-alpha (metabolism), Viral Envelope Proteins (metabolism), Virus Internalization.
- MESH :
- chemical , genetics : Peptidyl-Dipeptidase A, RNA, Small Interfering.
- chemical , metabolism : ADAM Proteins, Membrane Glycoproteins, Peptidyl-Dipeptidase A, RNA, Messenger, Tumor Necrosis Factor-alpha, Viral Envelope Proteins.
- chemical : ADAM17 Protein, Spike Glycoprotein, Coronavirus.
- genetics : Protein Structure, Tertiary, SARS Virus.
- physiology : SARS Virus.
- Animals, Cell Line, Humans, Mice, Sequence Deletion, Virus Internalization.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) is a high-risk infectious pathogen. In the proposed model of respiratory failure, SARS-CoV down-regulates its receptor, angiotensin-converting enzyme 2 (ACE2), but the mechanism involved is unknown. We found that the spike protein of SARS-CoV (SARS-S) induced TNF-alpha-converting enzyme (TACE)-dependent shedding of the ACE2 ectodomain. The modulation of TACE activity by SARS-S depended on the cytoplasmic domain of ACE2, because deletion mutants of ACE2 lacking the carboxyl-terminal region did not induce ACE2 shedding or TNF-alpha production. In contrast, the spike protein of HNL63-CoV (NL63-S), a CoV that uses ACE2 as a receptor and mainly induces the common cold, caused neither of these cellular responses. Intriguingly, viral infection, judged by real-time RT-PCR analysis of SARS-CoV mRNA expression, was significantly attenuated by deletion of the cytoplasmic tail of ACE2 or knock-down of TACE expression by siRNA. These data suggest that cellular signals triggered by the interaction of SARS-CoV with ACE2 are positively involved in viral entry but lead to tissue damage. These findings may lead to the development of anti-SARS-CoV agents.
DOI: 10.1073/pnas.0711241105
PubMed: 18490652
Affiliations:
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Murakami, Chikako" uniqKey="Nakai Murakami C" first="Chikako" last="Nakai-Murakami">Chikako Nakai-Murakami</name></author><author><name sortKey="Osawa, Yoshiaki" sort="Osawa, Yoshiaki" uniqKey="Osawa Y" first="Yoshiaki" last="Osawa">Yoshiaki Osawa</name></author><author><name sortKey="Tokunaga, Kenzo" sort="Tokunaga, Kenzo" uniqKey="Tokunaga K" first="Kenzo" last="Tokunaga">Kenzo Tokunaga</name></author><author><name sortKey="Sata, Tetsutaro" sort="Sata, Tetsutaro" uniqKey="Sata T" first="Tetsutaro" last="Sata">Tetsutaro Sata</name></author><author><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name></author><author><name sortKey="Sasazuki, Takehiko" sort="Sasazuki, Takehiko" uniqKey="Sasazuki T" first="Takehiko" last="Sasazuki">Takehiko Sasazuki</name></author><author><name sortKey="Ishizaka, Yukihito" sort="Ishizaka, Yukihito" uniqKey="Ishizaka Y" first="Yukihito" last="Ishizaka">Yukihito 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Yamamoto</name></author><author><name sortKey="Nakai Murakami, Chikako" sort="Nakai Murakami, Chikako" uniqKey="Nakai Murakami C" first="Chikako" last="Nakai-Murakami">Chikako Nakai-Murakami</name></author><author><name sortKey="Osawa, Yoshiaki" sort="Osawa, Yoshiaki" uniqKey="Osawa Y" first="Yoshiaki" last="Osawa">Yoshiaki Osawa</name></author><author><name sortKey="Tokunaga, Kenzo" sort="Tokunaga, Kenzo" uniqKey="Tokunaga K" first="Kenzo" last="Tokunaga">Kenzo Tokunaga</name></author><author><name sortKey="Sata, Tetsutaro" sort="Sata, Tetsutaro" uniqKey="Sata T" first="Tetsutaro" last="Sata">Tetsutaro Sata</name></author><author><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name></author><author><name sortKey="Sasazuki, Takehiko" sort="Sasazuki, Takehiko" uniqKey="Sasazuki T" first="Takehiko" last="Sasazuki">Takehiko Sasazuki</name></author><author><name sortKey="Ishizaka, Yukihito" sort="Ishizaka, Yukihito" uniqKey="Ishizaka Y" first="Yukihito" last="Ishizaka">Yukihito Ishizaka</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>ADAM Proteins (metabolism)</term><term>ADAM17 Protein</term><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Peptidyl-Dipeptidase A (genetics)</term><term>Peptidyl-Dipeptidase A (metabolism)</term><term>Protein Structure, Tertiary (genetics)</term><term>RNA, Messenger (metabolism)</term><term>RNA, Small Interfering (genetics)</term><term>SARS Virus (genetics)</term><term>SARS Virus (physiology)</term><term>Sequence Deletion</term><term>Spike Glycoprotein, Coronavirus</term><term>Tumor Necrosis Factor-alpha (metabolism)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Internalization</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (métabolisme)</term><term>Animaux</term><term>Délétion de séquence</term><term>Facteur de nécrose tumorale alpha (métabolisme)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Lignée cellulaire</term><term>Peptidyl-Dipeptidase A (génétique)</term><term>Peptidyl-Dipeptidase A (métabolisme)</term><term>Petit ARN interférent (génétique)</term><term>Protéine ADAM17</term><term>Protéines ADAM (métabolisme)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Pénétration virale</term><term>Souris</term><term>Structure tertiaire des protéines (génétique)</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptidyl-Dipeptidase A</term><term>RNA, Small Interfering</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>ADAM Proteins</term><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>RNA, Messenger</term><term>Tumor Necrosis Factor-alpha</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>ADAM17 Protein</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Protein Structure, Tertiary</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peptidyl-Dipeptidase A</term><term>Petit ARN interférent</term><term>Structure tertiaire des protéines</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term><term>Facteur de nécrose tumorale alpha</term><term>Glycoprotéines membranaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines ADAM</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Mice</term><term>Sequence Deletion</term><term>Virus Internalization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Délétion de séquence</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Lignée cellulaire</term><term>Protéine ADAM17</term><term>Pénétration virale</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) is a high-risk infectious pathogen. In the proposed model of respiratory failure, SARS-CoV down-regulates its receptor, angiotensin-converting enzyme 2 (ACE2), but the mechanism involved is unknown. We found that the spike protein of SARS-CoV (SARS-S) induced TNF-alpha-converting enzyme (TACE)-dependent shedding of the ACE2 ectodomain. The modulation of TACE activity by SARS-S depended on the cytoplasmic domain of ACE2, because deletion mutants of ACE2 lacking the carboxyl-terminal region did not induce ACE2 shedding or TNF-alpha production. In contrast, the spike protein of HNL63-CoV (NL63-S), a CoV that uses ACE2 as a receptor and mainly induces the common cold, caused neither of these cellular responses. Intriguingly, viral infection, judged by real-time RT-PCR analysis of SARS-CoV mRNA expression, was significantly attenuated by deletion of the cytoplasmic tail of ACE2 or knock-down of TACE expression by siRNA. These data suggest that cellular signals triggered by the interaction of SARS-CoV with ACE2 are positively involved in viral entry but lead to tissue damage. These findings may lead to the development of anti-SARS-CoV agents.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><noCountry><name sortKey="Ishizaka, Yukihito" sort="Ishizaka, Yukihito" uniqKey="Ishizaka Y" first="Yukihito" last="Ishizaka">Yukihito Ishizaka</name><name sortKey="Nakai Murakami, Chikako" sort="Nakai Murakami, Chikako" uniqKey="Nakai Murakami C" first="Chikako" last="Nakai-Murakami">Chikako Nakai-Murakami</name><name sortKey="Osawa, Yoshiaki" sort="Osawa, Yoshiaki" uniqKey="Osawa Y" first="Yoshiaki" last="Osawa">Yoshiaki Osawa</name><name sortKey="Sasazuki, Takehiko" sort="Sasazuki, Takehiko" uniqKey="Sasazuki T" first="Takehiko" last="Sasazuki">Takehiko Sasazuki</name><name sortKey="Sata, Tetsutaro" sort="Sata, Tetsutaro" uniqKey="Sata T" first="Tetsutaro" last="Sata">Tetsutaro Sata</name><name sortKey="Tokunaga, Kenzo" sort="Tokunaga, Kenzo" uniqKey="Tokunaga K" first="Kenzo" last="Tokunaga">Kenzo Tokunaga</name><name sortKey="Yamamoto, Naoki" sort="Yamamoto, Naoki" uniqKey="Yamamoto N" first="Naoki" last="Yamamoto">Naoki Yamamoto</name><name sortKey="Yamamoto, Norio" sort="Yamamoto, Norio" uniqKey="Yamamoto N" first="Norio" last="Yamamoto">Norio Yamamoto</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Haga, Shiori" sort="Haga, Shiori" uniqKey="Haga S" first="Shiori" last="Haga">Shiori Haga</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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