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Proteomic Analysis Uncovers Measles Virus Protein C Interaction with p65/iASPP/p53 Protein Complex

By Alice Meignié, Chantal Combredet, Marc Santolini, István A. Kovács, Thibaut Douché, Quentin Giai Gianetto, Hyeju Eun, Mariette Matondo, Yves Jacob, Regis Grailhe, Frédéric Tangy, Anastassia V. Komarova

Posted 09 May 2020
bioRxiv DOI: 10.1101/2020.05.08.084418

Viruses manipulate 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 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. To determine which host factors are targeted 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. 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 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/p53 protein complex that controls both cell death and innate immunity pathways.

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