Endosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy
Production of reactive oxygen species is an ancient antimicrobial mechanism, but its role in antiviral defense in mammals is unclear. Here, To et al. show that virus infection activates endosomal NOX2 oxidase and restricts TLR7 signaling, and that an endosomal NOX2 inhibitor decreases viral pathogen...
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Nature Portfolio
2017
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oai:doaj.org-article:1631134d108f482a9e7cb5b0a4cfdc772021-12-02T10:47:59ZEndosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy10.1038/s41467-017-00057-x2041-1723https://doaj.org/article/1631134d108f482a9e7cb5b0a4cfdc772017-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00057-xhttps://doaj.org/toc/2041-1723Production of reactive oxygen species is an ancient antimicrobial mechanism, but its role in antiviral defense in mammals is unclear. Here, To et al. show that virus infection activates endosomal NOX2 oxidase and restricts TLR7 signaling, and that an endosomal NOX2 inhibitor decreases viral pathogenicity.Eunice E. ToRoss VlahosRaymond LuongMichelle L. HallsPatrick C. ReadingPaul T. KingChristopher ChanGrant R. DrummondChristopher G. SobeyBrad R. S. BroughtonMalcolm R. StarkeyRenee van der SluisSharon R. LewinSteven BozinovskiLuke A. J. O’NeillTim QuachChristopher J. H. PorterDoug A. BrooksJohn J. O’LearyStavros SelemidisNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-17 (2017) |
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Science Q Eunice E. To Ross Vlahos Raymond Luong Michelle L. Halls Patrick C. Reading Paul T. King Christopher Chan Grant R. Drummond Christopher G. Sobey Brad R. S. Broughton Malcolm R. Starkey Renee van der Sluis Sharon R. Lewin Steven Bozinovski Luke A. J. O’Neill Tim Quach Christopher J. H. Porter Doug A. Brooks John J. O’Leary Stavros Selemidis Endosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy |
description |
Production of reactive oxygen species is an ancient antimicrobial mechanism, but its role in antiviral defense in mammals is unclear. Here, To et al. show that virus infection activates endosomal NOX2 oxidase and restricts TLR7 signaling, and that an endosomal NOX2 inhibitor decreases viral pathogenicity. |
format |
article |
author |
Eunice E. To Ross Vlahos Raymond Luong Michelle L. Halls Patrick C. Reading Paul T. King Christopher Chan Grant R. Drummond Christopher G. Sobey Brad R. S. Broughton Malcolm R. Starkey Renee van der Sluis Sharon R. Lewin Steven Bozinovski Luke A. J. O’Neill Tim Quach Christopher J. H. Porter Doug A. Brooks John J. O’Leary Stavros Selemidis |
author_facet |
Eunice E. To Ross Vlahos Raymond Luong Michelle L. Halls Patrick C. Reading Paul T. King Christopher Chan Grant R. Drummond Christopher G. Sobey Brad R. S. Broughton Malcolm R. Starkey Renee van der Sluis Sharon R. Lewin Steven Bozinovski Luke A. J. O’Neill Tim Quach Christopher J. H. Porter Doug A. Brooks John J. O’Leary Stavros Selemidis |
author_sort |
Eunice E. To |
title |
Endosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy |
title_short |
Endosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy |
title_full |
Endosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy |
title_fullStr |
Endosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy |
title_full_unstemmed |
Endosomal NOX2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy |
title_sort |
endosomal nox2 oxidase exacerbates virus pathogenicity and is a target for antiviral therapy |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doaj.org/article/1631134d108f482a9e7cb5b0a4cfdc77 |
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