Dataset Information

Npro protein interaction partners

ABSTRACT: The N-terminal protease Npro from pestiviruses has been shown to rapidly dismantle the innate immune response by targeting IRF3 for degradation, resulting in inhibition of apoptosis and interferon production. To understand it’s role in these different responses, we have identified multiple cellular factors that interact with this viral protein using mass spectrometry and proteomic analysis. Pull-down experiments were performed with Npro, and the samples were run on an SDS gel. Each lane was cut into 5-6 sclices and the slices were digested with trypsin. Peptides were extracted and analysed by LX-MSMS on an LTQ-Orbitrap (Thermo). Data were processed with MaxQuant (1.3.0.5) and searches performed with Mascot on the Sptrembl database (taxonomy human). All gel slices from one sample were merged in one Mascot search. Mascot results were imported into Scaffold 3.6.5.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hek-293 Cell

SUBMITTER: Gerhard Saalbach

LAB HEAD: Dr. Penny Powell

PROVIDER: PXD000115 | Pride | 2016-12-22

REPOSITORIES: pride

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Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.

Jefferson Matthew M Donaszi-Ivanov Andras A Pollen Sean S Dalmay Tamas T Saalbach Gerhard G Powell Penny P PP

Journal of virology 20140625 18

<h4>Unlabelled</h4>The viral N-terminal protease N(pro) of pestiviruses counteracts cellular antiviral defenses through inhibition of IRF3. Here we used mass spectrometry to identify a new role for N(pro) through its interaction with over 55 associated proteins, mainly ribosomal proteins and ribonucleoproteins, including RNA helicase A (DHX9), Y-box binding protein (YBX1), DDX3, DDX5, eIF3, IGF2BP1, multiple myeloma tumor protein 2, interleukin enhancer binding factor 3 (IEBP3), guanine nucleoti ...[more]

PMID: 24965446

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