DUSP1 regulates apoptosis and cell migration, but not the JIP1-protected cytokine response, during Respiratory Syncytial Virus and Sendai Virus infection

Alexa C. Robitaille; Elise Caron; Nicolas Zucchini; Espérance Mukawera; Damien Adam; Mélissa K. Mariani; Anaïs Gélinas; Audray Fortin; Emmanuelle Brochiero; Nathalie Grandvaux

To first assess a potential function of DUSP1, we analyzed DUSP1 expression during the course of SeV and RSV infection in A549 cells by immunoblot. DUSP1 was induced by about 4 fold at 6 h of RSV infection and was returned to basal levels at 24 h post-infection ( Figure 1A) . DUSP1 steady state levels remained unchanged during SeV infection ( Figure 1A) . Because DUSP1 turnover was previously reported to be affected by the ubiquitin-proteasome pathway 35 , we further analyzed DUSP1 levels during SeV and RSV infection in the presence of the 26S proteasome inhibitor MG132. In the presence of MG132, induction of DUSP1 is detectable in both infections and the overall DUSP1 levels were markedly increased compared to control cells ( Figure 1B) . These results imply that DUSP1 protein levels are induced in response to SeV and RSV infection and that DUSP1 is subjected to proteasome-mediated degradation.