Proteomic Analysis Uncovers Measles Virus Protein C Interaction With p65-iASPP Protein Complex.

Autor:	Meignié A; Viral Genomics and Vaccination Unit, Department of Virology, Institut Pasteur, CNRS UMR-3569, Paris, France; Université Paris Diderot, Sorbonne Paris Cité, Paris, France., Combredet C; Viral Genomics and Vaccination Unit, Department of Virology, Institut Pasteur, CNRS UMR-3569, Paris, France., Santolini M; Center for Research and Interdisciplinarity (CRI), Université de Paris, INSERM U1284, Paris, France; Network Science Institute and Department of Physics, Northeastern University, Boston, Massachusetts, USA., Kovács IA; Network Science Institute and Department of Physics, Northeastern University, Boston, Massachusetts, USA; Department of Physics and Astronomy, Northwestern University, Evanston, Illinois, USA; Department of Network and Data Science, Central European University, Budapest, Hungary., Douché T; Proteomics platform, Mass Spectrometry for Biology Unit (MSBio), Institut Pasteur, CNRS USR 2000, Paris, France., Gianetto QG; Proteomics platform, Mass Spectrometry for Biology Unit (MSBio), Institut Pasteur, CNRS USR 2000, Paris, France; Bioinformatics and Biostatistics Hub, Computational Biology Department, Institut Pasteur, CNRS USR 3756, Paris, France., Eun H; Technology Development Platform, Institut Pasteur Korea, Seongnam-si, Republic of Korea., Matondo M; Proteomics platform, Mass Spectrometry for Biology Unit (MSBio), Institut Pasteur, CNRS USR 2000, Paris, France., Jacob Y; Laboratory of Molecular Genetics of RNA Viruses, Institut Pasteur, CNRS UMR-3569, Paris, France., Grailhe R; Technology Development Platform, Institut Pasteur Korea, Seongnam-si, Republic of Korea., Tangy F; Viral Genomics and Vaccination Unit, Department of Virology, Institut Pasteur, CNRS UMR-3569, Paris, France. Electronic address: frederic.tangy@pasteur.fr., Komarova AV; Viral Genomics and Vaccination Unit, Department of Virology, Institut Pasteur, CNRS UMR-3569, Paris, France; Laboratory of Molecular Genetics of RNA Viruses, Institut Pasteur, CNRS UMR-3569, Paris, France. Electronic address: stasy@pasteur.fr.
Jazyk:	angličtina
Zdroj:	Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2021; Vol. 20, pp. 100049. Date of Electronic Publication: 2021 Jan 27.
DOI:	10.1016/j.mcpro.2021.100049
Abstrakt:	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 nonstructural 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 and the bioluminescence resonance energy transfer 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. Competing Interests: Conflict of interest The authors declare no competing interests. (Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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