tetano
Editor, Senior Moderator
Cell Rep
. 2022 Jan 25;38(4):110306.
doi: 10.1016/j.celrep.2022.110306.
Phosphoproteomic profiling of influenza virus entry reveals infection-triggered filopodia induction counteracted by dynamic cortactin phosphorylation
Annika Hunziker[SUP] 1 [/SUP], Irina Glas[SUP] 1 [/SUP], Marie O Pohl[SUP] 2 [/SUP], Silke Stertz[SUP] 3 [/SUP]
Affiliations
Abstract
Binding of influenza virus to its receptor triggers signaling cascades that reprogram the cell for infection. To elucidate global virus-induced changes to the cellular signaling landscape, we conducted a quantitative phosphoproteomic screen with human and avian influenza viruses. Proteins with functions in cell adhesion and cytoskeletal remodeling are overrepresented among the hits, and the majority of factors undergoing phosphorylation changes have a significant impact on infection efficiency. We show that influenza virus induces the formation of filopodia through Cdc42 signaling, which results in enhanced virus endocytosis. The host cell counteracts this mechanism with cortactin, a regulator of actin polymerization that becomes phosphorylated in response to virus binding and translocates to the cell cortex, where it limits filopodia formation and virus uptake. Overall, our study reveals the signaling cascades induced by influenza virus receptor engagement and uncovers virus-induced filopodia formation that is counteracted by the host cell.
Keywords: Cdc42 signalling; Endocytosis; Influenza virus; cortactin; filopodia; virus entry; virus-induced signalling.
. 2022 Jan 25;38(4):110306.
doi: 10.1016/j.celrep.2022.110306.
Phosphoproteomic profiling of influenza virus entry reveals infection-triggered filopodia induction counteracted by dynamic cortactin phosphorylation
Annika Hunziker[SUP] 1 [/SUP], Irina Glas[SUP] 1 [/SUP], Marie O Pohl[SUP] 2 [/SUP], Silke Stertz[SUP] 3 [/SUP]
Affiliations
- PMID: 35081340
- DOI: 10.1016/j.celrep.2022.110306
Abstract
Binding of influenza virus to its receptor triggers signaling cascades that reprogram the cell for infection. To elucidate global virus-induced changes to the cellular signaling landscape, we conducted a quantitative phosphoproteomic screen with human and avian influenza viruses. Proteins with functions in cell adhesion and cytoskeletal remodeling are overrepresented among the hits, and the majority of factors undergoing phosphorylation changes have a significant impact on infection efficiency. We show that influenza virus induces the formation of filopodia through Cdc42 signaling, which results in enhanced virus endocytosis. The host cell counteracts this mechanism with cortactin, a regulator of actin polymerization that becomes phosphorylated in response to virus binding and translocates to the cell cortex, where it limits filopodia formation and virus uptake. Overall, our study reveals the signaling cascades induced by influenza virus receptor engagement and uncovers virus-induced filopodia formation that is counteracted by the host cell.
Keywords: Cdc42 signalling; Endocytosis; Influenza virus; cortactin; filopodia; virus entry; virus-induced signalling.