Enhanced acetylation of alpha-tubulin in influenza A virus infected epithelial cells

FEBS Lett. 2011 Jan 3;585(1):128-32. doi: 10.1016/j.febslet.2010.11.023. Epub 2010 Nov 19.


Acetylated microtubules (AcMTs), a post-translationally modified form of microtubules, promote polarized protein transport. Here we report that influenza A virus (IAV) induces the acetylation of microtubules in epithelial cells. By employing specific inhibitors and siRNA we demonstrate Rho GTPase-mediated downregulation of tubulin deacetylase activity in IAV-infected cells, resulting in increased tubulin acetylation. Further, we demonstrate that depolymerization/deacetylation or enhanced acetylation of microtubules decreased or increased, respectively, the release of virions from infected cells. IAV assembly requires the polarized delivery of viral components to apical plasma membrane. Our findings suggest the potential involvement of AcMTs in polarized trafficking of IAV components.

MeSH terms

  • Acetylation
  • Animals
  • Blotting, Western
  • Cell Line
  • Down-Regulation
  • Epithelial Cells / metabolism*
  • Epithelial Cells / virology
  • Histone Deacetylase 6
  • Histone Deacetylases / genetics
  • Histone Deacetylases / metabolism
  • Host-Pathogen Interactions
  • Humans
  • Influenza A Virus, H1N1 Subtype / growth & development*
  • Influenza A Virus, H1N1 Subtype / physiology
  • Microtubules / metabolism*
  • RNA Interference
  • Tubulin / metabolism*
  • Virion / growth & development
  • rho GTP-Binding Proteins / genetics
  • rho GTP-Binding Proteins / metabolism


  • Tubulin
  • HDAC6 protein, human
  • Histone Deacetylase 6
  • Histone Deacetylases
  • rho GTP-Binding Proteins