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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection.

Efficient human immunodeficiency virus (HIV)-1 infection depends on multiple interactions between the viral gp41/gp120 envelope (Env) proteins and cell surface receptors. However, cytoskeleton-associated proteins that modify membrane dynamics may also regulate the formation of the HIV-mediated fusion pore and hence viral infection. Because the effects of HDAC6- tubulin deacetylase on cortical alpha-tubulin regulate cell migration and immune synapse organization, we explored the possible role of HDAC6 in HIV-1-envelope-mediated cell fusion and infection. The binding of the gp120 protein to CD4+-permissive cells increased the level of acetylated alpha-tubulin in a CD4-dependent manner. Furthermore, overexpression of active HDAC6 inhibited the acetylation of alpha-tubulin, and remarkably, prevented HIV-1 envelope-dependent cell fusion and infection without affecting the expression and codistribution of HIV-1 receptors. In contrast, knockdown of HDAC6 expression or inhibition of its tubulin deacetylase activity strongly enhanced HIV-1 infection and syncytia formation. These results demonstrate that HDAC6 plays a significant role in regulating HIV-1 infection and Env-mediated syncytia formation.[1]

References

  1. Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection. Valenzuela-Fernández, A., Alvarez, S., Gordon-Alonso, M., Barrero, M., Ursa, A., Cabrero, J.R., Fernández, G., Naranjo-Suárez, S., Yáñez-Mo, M., Serrador, J.M., Muñoz-Fernández, M.A., Sánchez-Madrid, F. Mol. Biol. Cell (2005) [Pubmed]
 
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