Severe Acute Respiratory Syndrome Coronavirus Viroporin 3a Activates the NLRP3 Inflammasome.
Identifieur interne : 000A94 ( Main/Exploration ); précédent : 000A93; suivant : 000A95Severe Acute Respiratory Syndrome Coronavirus Viroporin 3a Activates the NLRP3 Inflammasome.
Auteurs : I-Yin Chen [Japon] ; Miyu Moriyama [Japon] ; Ming-Fu Chang [Taïwan] ; Takeshi Ichinohe [Japon]Source :
- Frontiers in microbiology [ 1664-302X ] ; 2019.
Abstract
Nod-like receptor family, pyrin domain-containing 3 (NLRP3) regulates the secretion of proinflammatory cytokines interleukin 1 beta (IL-1β) and IL-18. We previously showed that influenza virus M2 or encephalomyocarditis virus (EMCV) 2B proteins stimulate IL-1β secretion following activation of the NLRP3 inflammasome. However, the mechanism by which severe acute respiratory syndrome coronavirus (SARS-CoV) activates the NLRP3 inflammasome remains unknown. Here, we provide direct evidence that SARS-CoV 3a protein activates the NLRP3 inflammasome in lipopolysaccharide-primed macrophages. SARS-CoV 3a was sufficient to cause the NLRP3 inflammasome activation. The ion channel activity of the 3a protein was essential for 3a-mediated IL-1β secretion. While cells uninfected or infected with a lentivirus expressing a 3a protein defective in ion channel activity expressed NLRP3 uniformly throughout the cytoplasm, NLRP3 was redistributed to the perinuclear space in cells infected with a lentivirus expressing the 3a protein. K+ efflux and mitochondrial reactive oxygen species were important for SARS-CoV 3a-induced NLRP3 inflammasome activation. These results highlight the importance of viroporins, transmembrane pore-forming viral proteins, in virus-induced NLRP3 inflammasome activation.
DOI: 10.3389/fmicb.2019.00050
PubMed: 30761102
Affiliations:
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regulates the secretion of proinflammatory cytokines interleukin 1 beta (IL-1β) and IL-18. We previously showed that influenza virus M2 or encephalomyocarditis virus (EMCV) 2B proteins stimulate IL-1β secretion following activation of the NLRP3 inflammasome. However, the mechanism by which severe acute respiratory syndrome coronavirus (SARS-CoV) activates the NLRP3 inflammasome remains unknown. Here, we provide direct evidence that SARS-CoV 3a protein activates the NLRP3 inflammasome in lipopolysaccharide-primed macrophages. SARS-CoV 3a was sufficient to cause the NLRP3 inflammasome activation. The ion channel activity of the 3a protein was essential for 3a-mediated IL-1β secretion. While cells uninfected or infected with a lentivirus expressing a 3a protein defective in ion channel activity expressed NLRP3 uniformly throughout the cytoplasm, NLRP3 was redistributed to the perinuclear space in cells infected with a lentivirus expressing the 3a protein. K<sup>+</sup> efflux and mitochondrial reactive oxygen species were important for SARS-CoV 3a-induced NLRP3 inflammasome activation. These results highlight the importance of viroporins, transmembrane pore-forming viral proteins, in virus-induced NLRP3 inflammasome activation.</div></front></TEI><affiliations><list><country><li>Japon</li><li>Taïwan</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Chen, I Yin" sort="Chen, I Yin" uniqKey="Chen I" first="I-Yin" last="Chen">I-Yin Chen</name></region><name sortKey="Ichinohe, Takeshi" sort="Ichinohe, Takeshi" uniqKey="Ichinohe T" first="Takeshi" last="Ichinohe">Takeshi Ichinohe</name><name sortKey="Moriyama, Miyu" sort="Moriyama, Miyu" uniqKey="Moriyama M" first="Miyu" last="Moriyama">Miyu Moriyama</name></country><country name="Taïwan"><noRegion><name sortKey="Chang, Ming Fu" sort="Chang, Ming Fu" uniqKey="Chang M" first="Ming-Fu" last="Chang">Ming-Fu Chang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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