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Disruption of Ebola NP0VP35 Inclusion Body-like Structures reduce Viral Infection.
Wu, Chao; Wagner, Nicole D; Moyle, Austin B; Feng, Annie; Sharma, Nitin; Stubbs, Sarah H; Donahue, Callie; Davey, Robert A; Gross, Michael L; Leung, Daisy W; Amarasinghe, Gaya K.
Affiliation
  • Wu C; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA. Electronic address: wuchao@szbl.ac.cn.
  • Wagner ND; Department of Chemistry, Washington University in St. Louis, St. Louis, MO, USA; Department of Medicine, Washington University School of Medicine in St. Louis, St. Louis, MO, USA.
  • Moyle AB; Department of Chemistry, Washington University in St. Louis, St. Louis, MO, USA.
  • Feng A; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA.
  • Sharma N; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA.
  • Stubbs SH; Department of Microbiology, National Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
  • Donahue C; Department of Microbiology, National Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
  • Davey RA; Department of Microbiology, National Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
  • Gross ML; Department of Chemistry, Washington University in St. Louis, St. Louis, MO, USA.
  • Leung DW; Department of Medicine, Washington University School of Medicine in St. Louis, St. Louis, MO, USA. Electronic address: dwleung@wustl.edu.
  • Amarasinghe GK; Department of Pathology and Immunology, Washington University School of Medicine in St. Louis, St. Louis, MO, USA. Electronic address: gamarasinghe@wustl.edu.
J Mol Biol ; 435(20): 168241, 2023 10 15.
Article in En | MEDLINE | ID: mdl-37598728
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Virus Replication / Inclusion Bodies / Hemorrhagic Fever, Ebola / Ebolavirus / Nucleoproteins Limits: Humans Language: En Journal: J Mol Biol Year: 2023 Document type: Article
Fulltext
Add to My VHL
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Virus Replication / Inclusion Bodies / Hemorrhagic Fever, Ebola / Ebolavirus / Nucleoproteins Limits: Humans Language: En Journal: J Mol Biol Year: 2023 Document type: Article