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Desipramine induces disorder in cholesterol-rich membranes: implications for viral trafficking

Kirsi Pakkanen1, Emppu Salonen, Anna R Mäkelä

  • 1Department of Biological and Environmental Science and Nanoscience Center, University of Jyväskylä, Finland. kirsi.i.pakkanen@jyu.fi

Physical Biology
|September 11, 2009
PubMed

Insights

Desipramine (DMI) disrupts cholesterol-rich cell membranes, impairing viral traffic and inhibiting canine parvovirus (CPV) proliferation by affecting endosomal function.

Area of Science:

  • Membrane biophysics
  • Virology
  • Computational biology

Background:

  • Cholesterol-rich membrane domains, or rafts, are crucial for cellular processes.
  • Antidepressants like desipramine (DMI) can interact with cell membranes.
  • Canine parvovirus (CPV) utilizes cellular membranes for entry and replication.

Purpose of the Study:

  • To investigate the effects of desipramine (DMI) on phospholipid bilayers and viral entry.
  • To elucidate the molecular mechanisms underlying DMI's interaction with membrane rafts.
  • To assess the impact of DMI on viral intracellular trafficking using CPV as a model.

Main Methods:

  • Atomistic molecular dynamics simulations to study DMI's effect on phospholipid bilayers.
  • Analysis of deuterium order parameter (S(CD)) and membrane area.
  • Inhibition assays using canine parvovirus (CPV) to study intracellular effects.

Main Results:

  • Desipramine (DMI) was observed to disorder cholesterol-rich phospholipid bilayers, decreasing the deuterium order parameter and increasing membrane area.
  • DMI destabilizes membrane rafts, suggesting a potential mechanism for its cellular effects.
  • DMI treatment caused retention of CPV in intracellular vesicles, inhibiting viral proliferation and indicating impaired viral traffic.

Conclusions:

  • Desipramine (DMI) disrupts the structure of cholesterol-rich membrane domains.
  • DMI interferes with intracellular viral trafficking, specifically affecting CPV.
  • The observed effects suggest DMI's potential to impair endosomal function through raft disruption, impacting viral penetration.

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