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Disruption of Ebola NP0VP35 Inclusion Body-like Structures reduce Viral Infection.


ABSTRACT: Viral inclusion bodies (IBs) are potential sites of viral replication and assembly. How viral IBs form remains poorly defined. Here we describe a combined biophysical and cellular approach to identify the components necessary for IB formation during Ebola virus (EBOV) infection. We find that the eNP0VP35 complex containing Ebola nucleoprotein (eNP) and viral protein 35 (eVP35), the functional equivalents of nucleoprotein (N) and phosphoprotein (P) in non-segmented negative strand viruses (NNSVs), phase separates to form inclusion bodies. Phase separation of eNP0VP35 is reversible and modulated by ionic strength. The multivalency of eVP35, and not eNP, is also critical for phase separation. Furthermore, overexpression of an eVP35 peptide disrupts eNP0VP35 complex formation, leading to reduced frequency of IB formation and limited viral infection. Together, our results show that upon EBOV infection, the eNP0VP35 complex forms the minimum unit to drive IB formation and viral replication.

SUBMITTER: Wu C 

PROVIDER: S-EPMC11312838 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature

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Disruption of Ebola NP<sup>0</sup>VP35 Inclusion Body-like Structures reduce Viral Infection.

Wu Chao C   Wagner Nicole D ND   Moyle Austin B AB   Feng Annie A   Sharma Nitin N   Stubbs Sarah H SH   Donahue Callie C   Davey Robert A RA   Gross Michael L ML   Leung Daisy W DW   Amarasinghe Gaya K GK  

Journal of molecular biology 20230819 20


Viral inclusion bodies (IBs) are potential sites of viral replication and assembly. How viral IBs form remains poorly defined. Here we describe a combined biophysical and cellular approach to identify the components necessary for IB formation during Ebola virus (EBOV) infection. We find that the eNP<sup>0</sup>VP35 complex containing Ebola nucleoprotein (eNP) and viral protein 35 (eVP35), the functional equivalents of nucleoprotein (N) and phosphoprotein (P) in non-segmented negative strand viru  ...[more]

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