APOBEC3F restricts PRRSV replication through its CD2 domain and interaction with host antiviral proteins

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Pengcheng Wang1, Xuan Hu1, Lang Tian1

  • 1Institute of Veterinary Immunology and Green Drugs, Veterinary Department in College of Animal Science, State Key Laboratory of Green Pesticide, Guizhou University, Guiyang 550025, China.

Veterinary Microbiology
|January 6, 2026
PubMed

Insights

Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F (APOBEC3F) protein suppresses Porcine reproductive and respiratory syndrome virus (PRRSV) replication. PRRSV proteins downregulate APOBEC3F, highlighting a potential therapeutic target for swine disease.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Porcine reproductive and respiratory syndrome virus (PRRSV) causes significant economic losses in the swine industry.
  • Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F (APOBEC3F) is a deaminase protein with known antiviral properties.
  • APOBEC3F is a component of cytoplasmic processing bodies (P-bodies).

Purpose of the Study:

  • To investigate the antiviral effects of APOBEC3F and its functional domains against PRRSV.
  • To identify PRRSV proteins that modulate APOBEC3F expression.
  • To explore potential host factors interacting with APOBEC3F during PRRSV infection.

Main Methods:

  • Overexpression and knockdown of APOBEC3F in porcine cells.
  • Measurement of PRRSV replication markers (transcription, protein expression, viral titers).
  • Analysis of APOBEC3F mRNA levels following PRRSV infection.
  • Immunoprecipitation-Mass Spectrometry (IP-MS) to identify interacting proteins.

Main Results:

  • APOBEC3F overexpression and its C-terminal deaminase domain (CD2) significantly inhibited PRRSV replication.
  • Knockdown of APOBEC3F led to enhanced PRRSV replication.
  • Several PRRSV non-structural proteins (NSP1α, NSP1β, NSP5, NSP7) and structural proteins (GP4, GP5, N) were found to downregulate APOBEC3F mRNA.
  • IP-MS identified potential interactors including DEAD-box helicases (DDX6, MOV10), suggesting APOBEC3F localization within P-bodies.

Conclusions:

  • APOBEC3F exhibits potent antiviral activity against PRRSV by suppressing viral replication.
  • PRRSV employs multiple viral proteins to counteract APOBEC3F-mediated host defense.
  • APOBEC3F likely functions in conjunction with P-body components to restrict PRRSV.
  • APOBEC3F represents a promising therapeutic target for controlling PRRSV infections.
Keywords:
APOBEC3FAntiviral mechanismCD2 domainHost-virus interactionPRRSV

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