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L-domain flanking sequences are important for host interactions and efficient budding of vesicular stomatitis virus

Takashi Irie1, Ronald N Harty

  • 1Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, 19104, USA.

Journal of Virology
|September 29, 2005
PubMed

Insights

Vesicular stomatitis virus (VSV) matrix protein

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Vesicular stomatitis virus (VSV) has PPPY and PSAP motifs in its matrix (M) protein.
  • The PPPY motif shows L-domain activity, but the PSAP motif does not in BHK-21 cells.

Purpose of the Study:

  • To investigate the role of amino acids flanking the PSAP motif in L-domain activity.
  • To understand how modifications affect VSV replication and budding.

Main Methods:

  • Generated VSV recombinants with mutations in sequences around the PSAP core motif.
  • Analyzed recombinant viruses for growth kinetics, budding efficiency, and host protein interactions.

Main Results:

  • Amino acid composition surrounding L-domain core motifs is critical for activity.
  • Mutations impact L-domain function and host protein interactions during VSV infection.

Conclusions:

  • The microenvironment of L-domain motifs significantly influences their function.
  • Understanding these interactions is key to controlling VSV replication.

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