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Coronavirus NSP5 protease cleaves CCDC50 to evade antiviral autophagy

Ke Li1,2, Hongyun Wei1,2, Wenqiu Yin1,2

  • 1State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.

Autophagy
|April 11, 2026
PubMed

Insights

The selective autophagy receptor CCDC50 restricts porcine deltacoronavirus (PDCoV) replication by degrading its envelope protein. However, PDCoV

Area of Science:

  • Virology
  • Cellular Biology
  • Immunology

Background:

  • Selective autophagy is crucial for innate antiviral immunity, utilizing specific receptors to target viral components for lysosomal degradation.
  • Porcine deltacoronavirus (PDCoV) employs its NSP5 protease to evade this essential cellular defense mechanism.

Purpose of the Study:

  • To investigate the role of the selective autophagy receptor CCDC50 in antiviral defense against PDCoV.
  • To elucidate the mechanism by which PDCoV evades CCDC50-mediated autophagy.

Main Methods:

  • Immunoblotting and immunoprecipitation assays to detect protein interactions and cleavage.
  • Autophagy assays to monitor the degradation of viral proteins.
  • Site-directed mutagenesis to identify critical residues for protein interaction and cleavage.

Main Results:

  • CCDC50 acts as a selective autophagy receptor, recognizing K63-linked polyubiquitinated PDCoV envelope (E) protein and mediating its autophagic degradation.
  • PDCoV NSP5 protease cleaves CCDC50 at a conserved site (glutamine 171), disrupting its interaction with ubiquitin and MAP1LC3/LC3.
  • This cleavage impairs CCDC50-mediated autophagic degradation of the E protein, thereby promoting viral replication.

Conclusions:

  • CCDC50 possesses a previously unrecognized antiviral function against coronaviruses.
  • Coronavirus NSP5 proteases promote viral infection by proteolytically inactivating CCDC50, a key receptor in antiviral autophagy.
Keywords:
CCDC50NSP5PDCoVcleavageselective autophagy

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