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Viroporin activity of the JC polyomavirus is regulated by interactions with the adaptor protein complex 3

Tadaki Suzuki1, Yasuko Orba, Yoshinori Makino

  • 1Division of Molecular Pathobiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo 001-0020, Japan.

Proceedings of the National Academy of Sciences of the United States of America
|October 30, 2013
PubMed

Insights

Human JC polyomavirus (JCV) agnoprotein interacts with host cell adaptor protein complex 3. This interaction disrupts cellular trafficking, leading to membrane permeabilization and regulating viroporin activity.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Interactions

Background:

  • Viroporins are viral proteins forming pores in host cell membranes, impacting cell physiology.
  • The role of host cell proteins in regulating viroporin activity is largely unknown.
  • Human JC polyomavirus (JCV) causes progressive multifocal leukoencephalopathy; its agnoprotein functions as a viroporin.

Purpose of the Study:

  • To investigate the interaction between JCV agnoprotein and host cell proteins.
  • To elucidate the mechanism by which agnoprotein influences cellular processes.
  • To understand how host factors regulate viroporin activity.

Main Methods:

  • Investigated the specific interaction between JCV agnoprotein and adaptor protein complex 3 (AP-3).
  • Analyzed the effect of this interaction on AP-3-mediated vesicular trafficking.
  • Examined the impact on protein localization and degradation pathways.

Main Results:

  • Demonstrated a specific interaction between JCV agnoprotein and the δ subunit of AP-3.
  • Showed that this interaction disrupts AP-3-mediated vesicular trafficking.
  • Revealed suppression of lysosomal degradation and promotion of cell surface transport, leading to membrane permeabilization.

Conclusions:

  • The JCV agnoprotein hijacks the host's AP-3 complex to alter vesicular trafficking.
  • This interaction allows agnoprotein to reach the cell surface, causing membrane permeabilization.
  • Presents a novel mechanism of virus-host interaction where the host regulates viroporin activity.
Keywords:
intracellular vesicular traffickingpathogen–host cell interaction

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