Proteomic Analysis of Measles Virus Protein C-Host Interactions in an Infectious Context Using Recombinant Viruses

Viruses manipulate central machineries of host cells to their advantage. They prevent host cell antiviral responses in order to create a favourable environment for their survival and propagation. Measles virus (MV) encodes two non-structural proteins MV-V and MV-C, proposed to counteract the host interferon response and to regulate cell death pathways in various functional assays. Several molecular mechanisms underlining MV-V regulation of innate immunity and cell death responses have been proposed, whereas MV-C host protein partners are less studied. We suggest that some cellular factors that are controlled by MV-C protein during viral replication could be components of innate immunity and the cell death pathways. In order to determine which host factors are hijacked by MV-C, we captured both direct and indirect host protein partners of MV-C protein. For this we used a strategy based on recombinant viruses expressing tagged viral proteins followed by affinity purification and a bottom-up mass spectrometry analysis. A list of host proteins specifically interacting with MV-C protein in different cell lines was identified.