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Published in Molecular & cellular proteomics : MCP - 27 Jan 2021

Meignié A, Combredet C, Santolini M, Kovács IA, Douché T, Gianetto QG, Eun H, Matondo M, Jacob Y, Grailhe R, Tangy F, Komarova AV,

Link to Pubmed [PMID] – 33515806

Link to DOI – S1535-9476(21)00022-010.1016/j.mcpro.2021.100049

Mol Cell Proteomics 2021 Jan; (): 100049

Viruses manipulate the central machineries of host cells to their advantage. They prevent host cell antiviral responses to create a favorable environment for their survival and propagation. Measles virus (MV) encodes two non-structural proteins MV-V and MV-C known to counteract the host interferon response and to regulate cell death pathways. Several molecular mechanisms underlining MV-V regulation of innate immunity and cell death pathways have been proposed, whereas MV-C host interacting proteins 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. To determine which host factors are targeted by MV-C, we captured both direct and indirect host interacting proteins 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. From the list of host proteins specifically interacting with MV-C protein in different cell lines, we selected the host targets that belong to immunity and cell death pathways for further validation. Direct protein interaction partners of MV-C were determined by applying protein complementation assay (PCA) and the bioluminescence resonance energy transfer (BRET) approach. As a result, we found that MV-C protein specifically interacts with p65/iASPP protein complex that controls both cell death and innate immunity pathways, and evaluated the significance of these host factors on virus replication.

https://pubmed.ncbi.nlm.nih.gov/33515806