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Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Viral glycoproteins require proper processing in the endoplasmic reticulum (ER) for infection.
  • Rotavirus outer capsid protein VP7 is an ER-resident protein whose N-terminal signal peptide cleavage mechanism was unknown.

Purpose of the Study:

  • To identify host factors involved in rotavirus VP7 processing and maturation.
  • To elucidate the role of identified host factors in rotavirus infection and assembly.

Main Methods:

  • Tandem affinity purification coupled with high-resolution mass spectrometry to identify VP7 interacting proteins.
  • CRISPR/Cas9 gene editing and siRNA for gene knockdown of signal peptidase complex (SPC) subunits.
  • Transmission electron microscopy (TEM) to analyze viral particle morphology.
  • Site-directed mutagenesis to investigate VP7-SPC interaction.

Main Results:

  • Members of the signal peptidase complex (SPC) were identified as host factors interacting with VP7.
  • Knockout or knockdown of SPC subunits significantly reduced infectious rotavirus titers.
  • Loss of SPC impaired VP7 signal peptide cleavage, leading to abnormal viral particles and defective virion maturation and assembly.
  • Residue E256 in VP7 was identified as a key site for SPC binding; mutation reduced viral infectivity.

Conclusions:

  • SPC is a novel regulator of rotavirus VP7 maturation and viral assembly.
  • SPC plays a critical role in rotavirus infection, independent of viral transcription, translation, or replication.
  • SPC represents a potential cellular target for broad-spectrum antiviral therapeutic development against rotavirus.