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Myristoylation of the RING finger Z protein is essential for arenavirus budding

Mar Perez1, Dori L Greenwald, Juan Carlos de la Torre

  • 1The Scripps Research Institute, IMM6, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.

Journal of Virology
|September 29, 2004
PubMed

Insights

N-terminal myristoylation of the arenavirus Z protein is crucial for viral budding. This modification, involving the addition of a myristoyl group, drives the release of new virus particles.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • The arenavirus small RING finger Z protein is essential for viral budding.
  • Despite lacking transmembrane domains, Z proteins associate with the inner plasma membrane.
  • Arenavirus Z proteins possess a conserved glycine at position 2, a potential myristoylation site.

Purpose of the Study:

  • To investigate the role of N-terminal myristoylation in arenavirus Z protein function.
  • To determine if myristoylation is essential for Z protein-mediated viral budding.

Main Methods:

  • Metabolic labeling with [(3)H]myristic acid to detect myristoylation.
  • Site-directed mutagenesis (G2A mutant) to abolish myristoylation.
  • Inhibition studies using a myristoylation inhibitor (2-hydroxymyristic acid).
  • Complementation assays by adding a myristoylation domain to the Z protein.

Main Results:

  • Wild-type Z protein incorporated myristic acid, while the G2A mutant did not.
  • The G2A mutation abolished Z protein-mediated budding and virus production.
  • Myristoylation inhibition and the G2A mutation significantly reduced virus-like particle formation and virus yield.
  • Restoration of budding in G2A mutants was achieved by adding an N-terminal myristoylation domain.

Conclusions:

  • N-terminal myristoylation of the arenavirus Z protein is a critical host-dependent step for viral budding.
  • Myristoylation directly influences Z protein membrane association and its ability to drive virus release.

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