Global quantitative proteomic analysis profiles host protein expression in response to Sendai virus infection

Abstract

Sendai virus (SeV) is an enveloped nonsegmented negative-strand RNA virus that belongs to the genus Respirovirus of the Paramyxoviridae family. As a model pathogen, SeV has been extensively studied to define the basic biochemical and molecular biologic properties of the paramyxoviruses. In addition, SeV-infected host cells were widely employed to uncover the mechanism of innate immune response. To identify proteins involved in the SeV infection process or the SeV-induced innate immune response process, system-wide evaluations of SeV-host interactions have been performed. cDNA microarray, siRNA screening and phosphoproteomic analysis suggested that multiple signaling pathways are involved in SeV infection process. Here, to study SeV-host interaction, a global quantitative proteomic analysis was performed on SeV-infected HEK 293T cells. A total of 4699 host proteins were quantified, with 742 proteins being differentially regulated. Bioinformatics analysis indicated that regulated proteins were mainly involved in "interferon type I (IFN-I) signaling pathway" and "defense response to virus," suggesting that these processes play roles in SeV infection. Further RNAi-based functional studies indicated that the regulated proteins, tripartite motif (TRIM24) and TRIM27, affect SeV-induced IFN-I production. Our data provided a comprehensive view of host cell response to SeV and identified host proteins involved in the SeV infection process or the SeV-induced innate immune response process.

Comprehensive Interactome Analysis Reveals that STT3B Is Required for N-Glycosylation of Lassa Virus Glycoprotein

“…The resulting peptides were separated from the beads by a magnetic rack and subjected to desalination and concentration by C 18 bonded Solid Phase Extraction Disks (Empore). Purified peptides were then subjected to electrospray ionization, followed by liquid chromatography-mass spectrometry (LC-MS) detection, as described previously (78). The obtained raw MA spectra were subjected to analysis by ProteinPilot version 5.0 for peptide sequence identification against the Swiss-Prot database (downloaded in 2017), which was set to human species restricted.…”

A Subcellular Quantitative Proteomic Analysis of Herpes Simplex Virus Type 1-Infected HEK 293T Cells

“…These proteins were selected based on a comparison with our previous quantitative analysis of RNA virus-infected host cells. CHCHD2 was also regulated by SeV [13], and IFITM3 was regulated by JEV [16], while TRIM27 was only regulated by HSV-1. HEK 293T cells were transfected with siRNAs against IFITM3 , CHCHD2 , and TRIM27 , and 24 h later, the cells were collected, and intracellular mRNAs were harvested for quantitative RT-PCR to test the knockdown efficiency of these siRNAs (Figure 5A).…”

“…A comparative analysis of the effects of SeV and HSV-1 infection on the host proteome has never been reported. Our previous SILAC-based quantitative analysis of SeV-infected HEK 293T cells highlighted several biological processes that may be involved in the viral replication process and virus-induced innate immune response [13]. In this study, we also compared the effects of SeV infection and HSV-1 infection on HEK 293T cells, and the biological processes regulated by both HSV-1 and SeV were identified.…”

Global Phosphoproteomics Analysis of IBRS-2 Cells Infected With Senecavirus A

“…Phosphoproteomics analysis of virus infection of host cells has been applied to influenza virus (Dapat et al, 2014), Sendai virus (Zhu et al, 2017a), porcine reproductive and respiratory syndrome virus (PRRSV; Luo et al, 2014a), and Gamma-herpesvirus (Stahl et al, 2013), among others. Phosphorylation is one of the most widespread PTMs, and it regulates numerous biological processes, including cell proliferation, growth, survival, and apoptosis (Stahl et al, 2013).…”