Us9-Independent Axonal Sorting and Transport of the Pseudorabies Virus Glycoprotein gM

R Kratchmarov1, L W Enquist1, M P Taylor2

  • 1Department of Molecular Biology, Princeton University, Princeton, New Jersey, USA.

Journal of Virology
|April 3, 2015
PubMed

Insights

Pseudorabies virus (PRV) glycoprotein M (gM) can be transported down axons independently of the Us9 protein. This Us9-independent mechanism highlights unique axonal transport properties of gM in viral infections.

Area of Science:

  • Neurovirology
  • Molecular Biology
  • Cell Biology

Background:

  • Axonal transport is crucial for neuronal function and can be hijacked by viruses.
  • Pseudorabies virus (PRV) assembly and axonal transport typically rely on the viral Us9 protein.
  • Understanding viral protein transport mechanisms is key to deciphering viral pathogenesis.

Purpose of the Study:

  • To investigate the mechanism of axonal localization for PRV glycoprotein M (gM).
  • To determine if gM axonal transport is dependent on the Us9 protein.
  • To characterize the properties of gM axonal transport compared to other viral proteins.

Main Methods:

  • Utilized fluorescently tagged gM (gM-mCherry) to visualize axonal transport in real-time.
  • Analyzed anterograde transport of gM assemblies within axons.
  • Employed Western blotting to detect unlabeled gM in isolated axons during infection with a Us9-null PRV strain.

Main Results:

  • Detected gM-mCherry assemblies undergoing anterograde transport in axons.
  • Confirmed the presence of unlabeled gM in isolated axons from Us9-null PRV infections.
  • Showed that glycoprotein B (gB) was not detected in axons under similar conditions, unlike gM.

Conclusions:

  • Viral glycoprotein M (gM) utilizes a Us9-independent pathway for axonal localization.
  • gM exhibits distinct axonal transport properties compared to other PRV proteins like gB.
  • This Us9-independent mechanism offers a novel perspective on viral protein trafficking in neurons.

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