The bovine herpesvirus type 1 envelope protein Us9 acidic domain is crucial for anterograde axonal transport

Vet Microbiol. 2011 Sep 28;152(3-4):270-9. doi: 10.1016/j.vetmic.2011.05.012. Epub 2011 May 13.

Abstract

In this study, we examined the functional role of bovine herpesvirus type 1 (BHV-1) Us9 acidic domain residues 83-90 in the anterograde axonal transport of the virus in calves (natural host), rabbits, and in cultured neurons. A mutant virus strain lacking Us9 residues 83-90 (BHV-1 Us9 Δ83-90) and the rescued virus (BHV-1 Us9 R83-90) replicated efficiently in the nasal and ocular epithelium during primary infection and established latency in the trigeminal ganglia (TG). However, upon reactivation from latency, only the BHV-1 Us9 R83-90 virus was detected in nasal and ocular swabs of animals. In compartmentalized, rabbit primary dorsal root ganglia (DRG) neuron cultures, the Us9-deleted BHV-1, BHV-1 Us9 Δ83-90 and BHV-1 Us9 R83-90 viruses were transported efficiently in the retrograde direction. However, only the BHV-1 Us9 R83-90 virus was transported in an anterograde direction. These studies suggested that the Us9 acidic domain residues located between 83 and 90 were required for axonal anterograde transport.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Axonal Transport*
  • Cattle
  • Cell Line
  • Ganglia, Spinal / virology
  • Herpesviridae Infections / veterinary*
  • Herpesviridae Infections / virology
  • Herpesvirus 1, Bovine / physiology*
  • Molecular Sequence Data
  • Neurons / virology
  • Protein Structure, Tertiary
  • Rabbits
  • Trigeminal Ganglion / virology
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / metabolism*

Substances

  • US9 protein, bovine herpesvirus 1
  • Viral Envelope Proteins