SrasV1, Ncbi, Merge, bibRecord, 001C64

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 : 001C64 ( Ncbi/Merge ); précédent : 001C63; suivant : 001C65

Modulation 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 Ishizaka

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2008.

RBID : pubmed:18490652

Descripteurs français

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

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001B36
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pubmed:18490652

Le document en format XML

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<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>
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Modulation of TNF-alpha-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-alpha production and facilitates viral entry.

Modulation of TNF-alpha-converting enzyme by the spike protein of SARS-CoV and ACE2 induces TNF-alpha production and facilitates viral entry.

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