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LD PROTEOMICS WITH TURBOT INFECTED BY EIB202

ABSTRACT: To investigate the impact of pathogenic immune stimulation on the lipid droplet (LD) proteome of turbot (Scophthalmus maximus), turbot were intraperitoneally injected with PBS (XA01292LQ_P), wild-type Edwardsiella piscicida EIB202 (XA01292LQ_W), or inactivated E. piscicida EIB202 (XA01292LQ_T). Liver tissues were collected, and LDs were extracted for 4D label-free quantitative proteomics analysis.

INSTRUMENT(S):

ORGANISM(S): Scophthalmus Maximus

TISSUE(S): Liver

SUBMITTER: Shuai Shao

LAB HEAD: SHAO SHUAI

PROVIDER: PXD047605 | Pride | 2024-11-21

REPOSITORIES: Pride

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Project description:Toxoplasma gondii is an obligate intracellular protozoan of severe threat to humans and livestock. Macrophages are the cell type preferentially infected by T. gondii in vivo. Protein phosphorylation is an important post-translational modification involved in diverse cellular functions. ARAF is member of the RAF family of serine/threonine protein kinases that is necessary for MAPK activation. Limited information is available about the level of protein phosphorylation variations and the roles of ARAF in macrophages with T. gondii infection, although our previous research found that ARAF knockout could reduce the apoptosis of porcine alveolar macrophages (3D4/21 cells) caused by T. gondii infection. Here, we used IMAC in combination with LC-MS/MS to profile the changes of phosphorylation in 3D4/21 cells and 3D4/21-ΔAraf cells upon Toxoplasma infection, respectively. A total of 1647 differentially expressed phosphorylated proteins (DEPPs) with 3876 differentially phosphorylated sites (DPSs) were identified in 3D4/21 cells with Toxoplasma infection (p3T group) when comparing 3D4/21 cells without parasite infection (pho3 group), and 959 DEPPs with1540 DPSs when comparing 3D4/21-ΔAraf cells with parasite infection (p3KT group). In addition, 552 DPSs corresponding to 406 DEPPs with the same phosphorylated sites were screened in the comparison p3T/pho3 vs. p3T/p3KT, which was identified as the DPSs and DEPPs related with ARAF. Remarkable functional properties of the DEPPs were discovered by GO analysis, KEGG pathway analysis, and STRING analysis. Of 406 DEPPs related with ARAF, 40 DEPPs corresponding to 57 DPSs involved in the apoptosis of 3D4/21 cells during Toxoplasma infection. Further analysis showed that the phosphorylation levels of MED1at serine1418, JUN at serine 73, MYC at serine 154, MCL1 at serine 65, and BAD at serine115 were upregulated in p3T, but downregulated in p3KT, suggesting that ARAF regulate phosphorylation of these sites to modulate the apoptosis of macrophages induced by Toxoplasma infection. These results revealed distinct responses of macrophages to Toxoplasma infection and the potential roles of ARAF in fighting against infection via phosphorylation of crucial proteins.

			Action	DRS
	XA01292LQ_P1.msf	Msf
	XA01292LQ_P1.raw	Raw
	XA01292LQ_P2.raw	Raw
	XA01292LQ_P3.raw	Raw
	XA01292LQ_T1.raw	Raw

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LD PROTEOMICS WITH TURBOT INFECTED BY EIB202

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