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

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

doi:10.1016/J.MCPRO.2021.100049

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

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^*

^*Corresponding author for this work

Physics and Astronomy

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

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.

Original language	English (US)
Article number	100049
Journal	Molecular and Cellular Proteomics
Volume	20
DOIs	https://doi.org/10.1016/J.MCPRO.2021.100049
State	Published - 2021

Funding

Acknowledgments—We thank Dr Kaoru Takeuchi and Dr Chantal Rabourdin-Combe for anti-C rAb polyclonal antibody and anti-N monoclonal antibody, respectively. We thank Dr.Hervé Bourhy from Lyssavirus Epidemiology and Neuropathology Laboratory of Institut Pasteur for providing us pYFP-p65 plasmid that contains EYFP reporter gene fused to p65. We thank all members of the Viral Genomics and Vaccination Unit and Laboratory of Molecular Genetics of RNA Viruses for their critical discussion, Dr Atousa Arbabian for technical support with experiments, Dr Dmitry Trubetskoy for the help with data representation, and Dr Aleksandr Barinov and Dr Caroline Demeret for critical reading. This work was supported by ANR 16 CE18 0016 01 Tangy ONCOMEVAX, the Institut Pasteur, and CNRS. We thank Dr Kaoru Takeuchi and Dr Chantal Rabourdin-Combe for anti-C rAb polyclonal antibody and anti-N monoclonal antibody, respectively. We thank Dr.Hervé Bourhy from Lyssavirus Epidemiology and Neuropathology Laboratory of Institut Pasteur for providing us pYFP-p65 plasmid that contains EYFP reporter gene fused to p65. We thank all members of the Viral Genomics and Vaccination Unit and Laboratory of Molecular Genetics of RNA Viruses for their critical discussion, Dr Atousa Arbabian for technical support with experiments, Dr Dmitry Trubetskoy for the help with data representation, and Dr Aleksandr Barinov and Dr Caroline Demeret for critical reading. This work was supported by ANR 16 CE18 0016 01 Tangy ONCOMEVAX, the Institut Pasteur, and CNRS. This work was supported by National Research Agency (ANR 16 CE18 0016 01 Tangy ONCOMEVAX), the Institut Pasteur, and the French National Centre for Scientific Research (CNRS). A. M., PhD, was supported by Région ile de France (IDF DIM 2016) and Institut Pasteur Calmette and Yersin 2019 grant. Funding and additional information—This work was supported by National Research Agency (ANR 16 CE18 0016 01 Tangy ONCOMEVAX), the Institut Pasteur, and the French National Centre for Scientific Research (CNRS). A. M., PhD, was supported by Région ile de France (IDF DIM 2016) and Institut Pasteur Calmette and Yersin 2019 grant.

Keywords

Measles virus (MV) is a member of the genus Morbillivirus of the family Paramyxoviridae. This enveloped virus with a

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Molecular Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/J.MCPRO.2021.100049

Cite this

@article{aaab09d0f47b46de977fba4293337e73,

title = "Proteomic Analysis Uncovers Measles Virus Protein C Interaction with p65–iASPP Protein Complex",

abstract = "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.",

keywords = "Measles virus (MV) is a member of the genus Morbillivirus of the family Paramyxoviridae. This enveloped virus with a",

author = "Alice Meigni{\'e} and Chantal Combredet and Marc Santolini and Kov{\'a}cs, {Istv{\'a}n A.} and Thibaut Douch{\'e} and Gianetto, {Quentin Giai} and Hyeju Eun and Mariette Matondo and Yves Jacob and Regis Grailhe and Fr{\'e}d{\'e}ric Tangy and Komarova, {Anastassia V.}",

note = "Publisher Copyright: {\textcopyright} 2021 THE AUTHORS.",

year = "2021",

doi = "10.1016/J.MCPRO.2021.100049",

language = "English (US)",

volume = "20",

journal = "Molecular and Cellular Proteomics",

issn = "1535-9476",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

}

TY - JOUR

T1 - Proteomic Analysis Uncovers Measles Virus Protein C Interaction with p65–iASPP Protein Complex

AU - Meignié, Alice

AU - Combredet, Chantal

AU - Santolini, Marc

AU - Kovács, István A.

AU - Douché, Thibaut

AU - Gianetto, Quentin Giai

AU - Eun, Hyeju

AU - Matondo, Mariette

AU - Jacob, Yves

AU - Grailhe, Regis

AU - Tangy, Frédéric

AU - Komarova, Anastassia V.

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

KW - Measles virus (MV) is a member of the genus Morbillivirus of the family Paramyxoviridae. This enveloped virus with a

UR - http://www.scopus.com/inward/record.url?scp=85102687543&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85102687543&partnerID=8YFLogxK

U2 - 10.1016/J.MCPRO.2021.100049

DO - 10.1016/J.MCPRO.2021.100049

M3 - Article

C2 - 33515806

AN - SCOPUS:85102687543

SN - 1535-9476

VL - 20

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

M1 - 100049

ER -

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

Abstract

Funding

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this