Septins suppress the release of vaccinia virus from infected cells
journal contributionposted on 07.09.2020, 11:31 by Julia Pfanzelter, Serge Mostowy, Michael Way
Septins are conserved components of the cytoskeleton that play important roles in many fundamental cellular processes including division, migration, and membrane trafficking. Septins can also inhibit bacterial infection by forming cage-like structures around pathogens such as Shigella We found that septins are recruited to vaccinia virus immediately after its fusion with the plasma membrane during viral egress. RNA interference-mediated depletion of septins increases virus release and cell-to-cell spread, as well as actin tail formation. Live cell imaging reveals that septins are displaced from the virus when it induces actin polymerization. Septin loss, however, depends on the recruitment of the SH2/SH3 adaptor Nck, but not the activity of the Arp2/3 complex. Moreover, it is the recruitment of dynamin by the third Nck SH3 domain that displaces septins from the virus in a formin-dependent fashion. Our study demonstrates that septins suppress vaccinia release by "entrapping" the virus at the plasma membrane. This antiviral effect is overcome by dynamin together with formin-mediated actin polymerization.
Actin-Related Protein 2-3 ComplexAdaptor Proteins, Signal TransducingCell MembraneClathrinDynaminsHeLa CellsHumansOncogene ProteinsPhosphorylationRNA InterferenceSeptinsSignal TransductionVacciniaVirus ReleaseHela CellsWay FC001209Developmental Biology06 Biological Sciences11 Medical and Health Sciences