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A lipid receptor sorts polyomavirus from the endolysosome to the endoplasmic reticulum to cause infection

Mengding Qian1, Dawen Cai, Kristen J Verhey

  • 1Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, Michigan, United States of America.

Plos Pathogens
|June 9, 2009
PubMed

Insights

Murine polyomavirus (Py) uses ganglioside GD1a to target the endoplasmic reticulum (ER) via a novel endolysosome-to-ER pathway. This lipid-regulated transport is crucial for viral infection initiation.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Intracellular virus transport mechanisms remain poorly understood.
  • Murine polyomavirus (Py) infects cells by reaching the nucleus via the endoplasmic reticulum (ER).

Purpose of the Study:

  • To elucidate the transport pathway of Py from its entry point to the ER.
  • To determine the role of ganglioside GD1a in Py intracellular trafficking.

Main Methods:

  • Utilized cell-based assays to track Py transport.
  • Investigated the effect of pH on Py conformational changes.
  • Employed antibody-coated artificial particles to assess GD1a's targeting function.

Main Results:

  • Py is initially transported to the endolysosome, where low pH induces conformational changes.
  • Ganglioside GD1a binding, not viral entry, mediates Py sorting from endosomes/lysosomes to the ER.
  • Artificial particles coated with GD1a antibodies also traffic to the ER.

Conclusions:

  • A novel endolysosome-to-ER transport pathway regulated by ganglioside GD1a is demonstrated.
  • Ganglioside binding serves as a potential general mechanism for ER targeting of viruses.
  • The findings provide a rationale for Py's endolysosomal transit before ER entry.

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