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Updated: Nov 23, 2025

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Palmitoylation of the Bovine Foamy Virus Envelope Glycoprotein Is Required for Viral Replication

Keli Chai1, Zhaohuan Wang1, Yali Xu1

  • 1Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, China.

Viruses
|December 30, 2020
PubMed

Insights

Foamy virus (FV) envelope glycoproteins are palmitoylated, a modification crucial for viral replication. This study identifies specific palmitoylation sites on bovine foamy virus (BFV) Env, demonstrating its essential role in viral processes.

Area of Science:

  • Virology
  • Molecular Biology
  • Post-translational Modifications

Background:

  • Membrane proteins of enveloped viruses often undergo palmitoylation.
  • Palmitoylation critically influences viral protein function and replication.

Purpose of the Study:

  • To investigate the palmitoylation of foamy virus (FV) envelope (Env) glycoprotein.
  • To determine the role of palmitoylation in bovine foamy virus (BFV) replication.

Main Methods:

  • Identified palmitoylation sites on BFV Env (BEnv) using DHHC motif analysis.
  • Utilized site-directed mutagenesis (C58S, C59S) to assess functional impact.
  • Quantified cell surface expression, subviral particle (SVP) egress, and membrane fusion activity.

Main Results:

  • Bovine foamy virus Env (BEnv) is palmitoylated at cysteine residues C58 and C59 by DHHC proteins.
  • Mutations C58S and C58/59S significantly impaired BEnv cell surface expression, SVP egress, and membrane fusion.
  • These impairments ultimately inhibited bovine foamy virus replication.

Conclusions:

  • Palmitoylation is a key regulatory mechanism for BFV Env function.
  • The palmitoylation of BEnv at C58 and C59 is essential for efficient BFV replication.
Keywords:
BDHHC20BDHHC3bovine foamy viruscell surfaceenvelope glycoproteinmembrane fusionpalmitoylationreplicationsubviral particle

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