Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

ZIKA Virus Envelope Protein Forms Disulfide Bond-Dependent Polymers: Evidence for A Redox Imbalance during Infection

Grégorie Lebeau
* ,
Jonathan Turpin
* ,
Etienne Frumence
,
Daed El Safadi
,
Wissal harrabi
,
Philippe Desprès
ORCID logo ,
Pascale Krejbich-Trotot
* ORCID logo ,
wildriss viranaïcken
* ORCID logo
Version 1 : Received: 1 April 2022 / Approved: 6 April 2022 / Online: 6 April 2022 (05:24:41 CEST)

A peer-reviewed article of this Preprint also exists.

Lebeau, G.; Turpin, J.; Frumence, E.; El Safadi, D.; Harrabi, W.; Desprès, P.; Krejbich-Trotot, P.; Viranaïcken, W. Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein. Viruses 2022, 14, 1131. Lebeau, G.; Turpin, J.; Frumence, E.; El Safadi, D.; Harrabi, W.; Desprès, P.; Krejbich-Trotot, P.; Viranaïcken, W. Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein. Viruses 2022, 14, 1131.

Abstract

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 form native disulfide bonds in proteins. ZIKA virus (ZIKV) has ability to induce persistent ER stress leading to 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 redox state leading to aggregation of viral envelope protein as amyloid-like structures in the infected cells.

Keywords

Zika virus; unfolded protein response; ER stress; oligomer; disulfide bond amyloid aggregates

Subject

Biology and Life Sciences, Virology

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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