Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein
Flaviviruses replicate in membrane factories associated with the endoplasmic reticulum (ER). Significant levels of flavivirus viral protein accumulation contribute to ER stress. As a consequence, the host cell exhibits an Unfolded Protein Response (UPR), subsequently stimulating appropriate cellular...
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MDPI AG
2022-05-01
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Online Access: | https://www.mdpi.com/1999-4915/14/6/1131 |
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author | Grégorie Lebeau Jonathan Turpin Etienne Frumence Daed El Safadi Wissal Harrabi Philippe Desprès Pascale Krejbich-Trotot Wildriss Viranaïcken |
author_facet | Grégorie Lebeau Jonathan Turpin Etienne Frumence Daed El Safadi Wissal Harrabi Philippe Desprès Pascale Krejbich-Trotot Wildriss Viranaïcken |
author_sort | Grégorie Lebeau |
collection | DOAJ |
description | Flaviviruses replicate in membrane factories associated with the endoplasmic reticulum (ER). Significant levels of flavivirus viral protein accumulation contribute to ER stress. As a consequence, the host cell exhibits an Unfolded Protein Response (UPR), subsequently stimulating appropriate cellular responses such as adaptation, autophagy or apoptosis. The correct redox conditions of this compartment are essential to forming native disulfide bonds in proteins. Zika virus (ZIKV) has the ability to induce persistent ER stress leading to the activation of UPR pathways. In this study, we wondered whether ZIKV affects the redox balance and consequently the oxidative protein folding in the ER. We found that ZIKV replication influences the redox state, leading to the aggregation of the viral envelope protein as amyloid-like structures in the infected cells. |
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id | doaj.art-41e267bf2a5e41dbb042b29d2560f24d |
institution | Directory Open Access Journal |
issn | 1999-4915 |
language | English |
last_indexed | 2024-03-09T22:15:11Z |
publishDate | 2022-05-01 |
publisher | MDPI AG |
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series | Viruses |
spelling | doaj.art-41e267bf2a5e41dbb042b29d2560f24d2023-11-23T19:24:03ZengMDPI AGViruses1999-49152022-05-01146113110.3390/v14061131Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope ProteinGrégorie Lebeau0Jonathan Turpin1Etienne Frumence2Daed El Safadi3Wissal Harrabi4Philippe Desprès5Pascale Krejbich-Trotot6Wildriss Viranaïcken7PIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FrancePIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FrancePIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FrancePIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FrancePIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FrancePIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FrancePIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FrancePIMIT, Processus Infectieux en Milieu Insulaire Tropical, Université de La Réunion, INSERM UMR 1187, CNRS 9192, IRD 249, Plateforme CYROI, 97490 Sainte-Clotilde, Ile de La Réunion, FranceFlaviviruses replicate in membrane factories associated with the endoplasmic reticulum (ER). Significant levels of flavivirus viral protein accumulation contribute to ER stress. As a consequence, the host cell exhibits an Unfolded Protein Response (UPR), subsequently stimulating appropriate cellular responses such as adaptation, autophagy or apoptosis. The correct redox conditions of this compartment are essential to forming native disulfide bonds in proteins. Zika virus (ZIKV) has the ability to induce persistent ER stress leading to the activation of UPR pathways. In this study, we wondered whether ZIKV affects the redox balance and consequently the oxidative protein folding in the ER. We found that ZIKV replication influences the redox state, leading to the aggregation of the viral envelope protein as amyloid-like structures in the infected cells.https://www.mdpi.com/1999-4915/14/6/1131Zika virusunfolded protein responseER stressoligomerdisulfide bondamyloid aggregates |
spellingShingle | Grégorie Lebeau Jonathan Turpin Etienne Frumence Daed El Safadi Wissal Harrabi Philippe Desprès Pascale Krejbich-Trotot Wildriss Viranaïcken Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein Viruses Zika virus unfolded protein response ER stress oligomer disulfide bond amyloid aggregates |
title | Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein |
title_full | Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein |
title_fullStr | Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein |
title_full_unstemmed | Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein |
title_short | Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein |
title_sort | evidence of redox imbalance during zika virus infection promoting the formation of disulfide bond dependent oligomers of the envelope protein |
topic | Zika virus unfolded protein response ER stress oligomer disulfide bond amyloid aggregates |
url | https://www.mdpi.com/1999-4915/14/6/1131 |
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