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Cysteine Redox State Governs the Condensation Pathway of Hendra Virus W Protein and Differentially Impacts Type I IFN

Frank Gondelaud1, Alexandre Lalande2, Giulia Pesce1

  • 1Laboratoire Architecture Et Fonction des Macromolécules Biologiques (AFMB), UMR 7257, Aix Marseille University and Centre National De La Recherche Scientifique (CNRS), Marseille, France.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|July 17, 2026
PubMed

Insights

Hendra and Nipah virus W proteins form flexible fibrils or amorphous aggregates, controlled by cysteine oxidation. This redox switch influences viral immune evasion strategies within host cells.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Hendra virus (HeV) and Nipah virus (NiV) are zoonotic Paramyxoviridae viruses.
  • Their W proteins are crucial for evading host antiviral responses.
  • Previous work demonstrated HeV W protein forms flexible, curved fibrils in vitro.

Purpose of the Study:

  • To investigate the role of cysteine oxidation state in HeV W protein self-assembly.
  • To determine the structural requirements for HeV W protein fibrillation.
  • To examine the cellular localization and function of HeV W protein condensates.

Main Methods:

  • In vitro biochemical assays to study protein aggregation and fibrillation.
  • Site-directed mutagenesis to probe the role of specific residues and cysteine oxidation.
  • Cellular imaging and biochemical assays to analyze nuclear condensate formation and function.
  • NF-κB and interferon pathway activity assays.

Main Results:

  • Cysteine oxidation state acts as a molecular switch, determining the formation of amorphous aggregates versus flexible fibrils.
  • Residues 2 to 29 of HeV W protein are essential for fibrillation.
  • HeV W protein self-assembles in cellula, forming distinct nuclear condensates dependent on cysteine redox state.
  • Impaired condensate formation affects NF-κB inhibition and enhances interferon response repression via STAT1 binding.

Conclusions:

  • The redox state of cysteine residues regulates HeV W protein assembly into distinct structures.
  • Cellular condensation of HeV W protein is crucial for its function in modulating host antiviral pathways.
  • Understanding these mechanisms provides insights into viral immune evasion strategies.
Keywords:
cysteinesfibrilshenipavirusesinnate immune responseintrinsically disordered proteinsreactive oxygen species

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