%0 Journal Article %A Wang, Zhimin %A Kim, Jae Il %A Frilot, Nicole %A Daaka, Yehia %T Dynamin2 S-nitrosylation regulates adenovirus type 5 infection of epithelial cells %D 2012 %J Journal of General Virology, %V 93 %N 10 %P 2109-2117 %@ 1465-2099 %R https://doi.org/10.1099/vir.0.042713-0 %I Microbiology Society, %X Dynamin2 is a large GTPase that regulates vesicle trafficking, and the GTPase activity of dynamin2 is required for the multistep process of adenovirus infection. Activity of dynamin2 may be regulated by post-translational phosphorylation and S-nitrosylation modifications. In this study, we demonstrate a role for dynamin2 S-nitrosylation in adenovirus infection of epithelial cells. We show that adenovirus serotype 5 (Ad5) infection augments production of nitric oxide (NO) in epithelial cells and causes the S-nitrosylation of dynamin2, mainly on cysteine 86 (C86) and 607 (C607) residues. Forced overexpression of dynamin2 bearing C86A and/or C607A mutations decreases Ad5 infection. Diminishing NO synthesis by RNAi-induced knockdown of endogenous endothelial NO synthase (eNOS) expression attenuates virus infection of target cells. Ad5 infection promotes the kinetically dynamic S-nitrosylation of dynamin2 and eNOS: there is a rapid decrease in eNOS S-nitrosylation and a concomitant increase in the dynamin2 S-nitrosylation. These results support the hypothesis that dynamin2 S-nitrosylation following eNOS activation facilitates adenovirus infection of host epithelial cells. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.042713-0