Related Experiment Video

Updated: Jan 24, 2026

Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins
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Acyl-PEGyl Exchange Gel Shift Assay for Quantitative Determination of Palmitoylation of Brain Membrane Proteins

Published on: March 29, 2020

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Palmitoylation of the human cytomegalovirus tegument protein pp28 facilitates virus release

Jae Bong Lee1,2, Naeok Koo1,2, Ji Min Park1,2

  • 1Department of Biomedical Sciences, Yonsei University College of Medicine, Seoul, Republic of Korea.

Plos Pathogens
|January 22, 2026
PubMed

Insights

Palmitoylation, a lipid modification, is crucial for the human cytomegalovirus (HCMV) pp28 protein's stability and function. This modification ensures proper viral assembly and the release of infectious virions.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Tegument proteins are vital for human cytomegalovirus (HCMV) assembly and maturation.
  • pp28 (UL99) is a key tegument protein essential for cytoplasmic envelopment and trafficking to the viral assembly compartment (vAC).

Purpose of the Study:

  • To investigate the role of protein lipidation, specifically palmitoylation, in the function of HCMV pp28 protein.
  • To determine the impact of impaired palmitoylation on pp28 stability, localization, and viral replication.

Main Methods:

  • Site-directed mutagenesis was used to disrupt conserved cysteine residues in pp28.
  • Acyl-resin assisted capture (acyl-RAC) assays identified palmitoylation sites.
  • Confocal imaging and proteasome inhibition assays assessed protein stability and localization.
  • Recombinant HCMVs with pp28 mutants were generated to evaluate viral titers.

Main Results:

  • Palmitoylation of pp28 occurs at N-terminal cysteine residues (Cys6, Cys10, Cys11).
  • Disruption of palmitoylation sites impairs pp28 stability, leading to increased degradation.
  • Palmitoylation-deficient pp28 fails to localize correctly to ERGIC-derived membranes and reduces infectious virion release.
  • HCMV mutants with impaired pp28 palmitoylation show reduced extracellular viral titers.

Conclusions:

  • Palmitoylation is a critical post-translational modification for HCMV pp28 function, stability, and proper subcellular targeting.
  • This lipidation is essential for efficient virion maturation and egress, highlighting its broader significance in herpesvirus assembly.
  • The findings underscore the importance of tegument protein lipidation in the viral lifecycle.

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