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Phosphorylated proteomics data of protein kinase MoCK2 in Magnaporthe oryzae

ABSTRACT: In Magnaporthe oryzae, the protein kinase MoCK2 plays a crucial role in the pathogenicity of the fungus. Since knockout mutants of its regulatory subunits completely lose pathogenicity, analyzing differences in protein phosphorylation between mutants and wild-type strains and identifying proteins interacting with MoCK2 are essential steps to elucidate the underlying mechanisms by which MoCK2 regulates pathogenicity. This investigation provides critical theoretical support for subsequent efforts to decipher the molecular basis of pathogenicity development.

INSTRUMENT(S):

ORGANISM(S): Pyricularia Oryzae 70-15

TISSUE(S): Mycelium

SUBMITTER: Lianhu Zhang

LAB HEAD: Lianhu Zhang

PROVIDER: PXD066274 | Pride | 2025-10-07

REPOSITORIES: Pride

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Project description:Clinical therapeutic human serum albumin (HSA) preparations are manufactured by human plasma from donors and contain some miscellaneous proteins (MPs) except albumin. Multiple studies have demonstrated significant variations in the extent of post-translation modifications, redox states, and antioxidant capacities among HSA preparations from different manufacturers. However, these studies have primarily focused on the albumin molecule itself and have not conducted detailed analysis and comparison of the MPs present in HSA preparations. While there have been a few studies that have reported on the presence of MPs in commercial HSA preparations, research in this area is still relatively scarce. In this study, we employed 4D Label-Free quantitative proteomic technology to conduct identification and analysis of MPs in preparations of human plasma-derived HSA (pHSA) from 6 distinct manufacturers; Additionally, we investigated MPs in recombinant HSA (rHSA) preparations obtained through expression in yeast and rice. There were total 456 different MPs identified in 6 pHSA samples and 96 MPs were detected in all pHSA samples. 52 MPs in the rHSA (expressed in yeast) sample and 152 in the rHSA (expressed in rice) were identified. Haptoglobin, Hemopexin and Transthyretin included the top 8 MPs with the highest relative abundance detected in every pHSA preparations in this study. Bioinformatics (including GO, COG/KOG, KEGG, protein−protein interactions, etc.) analysis showed that the MPs identified in pHSA were basically involved in endopeptidase inhibitor activity, complement and coagulation cascades, biosynthesis of amino acids and cholesterol metabolism. Validation results demonstrated that HP, HPX, TF and TTR could be detected in pHSA but not in rHSA, which were consistent with 4D Label-Free quantitative proteomic results. Compared with previous studies, more trace MPs were detected in pHSA and rHSA preparations by 4D Label-Free quantitative proteomic technology. This could provide a new approach for high-throughput detection of trace MPs in HSA preparations.

Project description:This study aims to analyze and compare the post-translational modification differences between human plasma- and genetic recombination-derived human serum albumin (HSA) in clinical treatments in China. 6 different post-translational modifications, including acetylation, succinylation, crotonylation, phosphorylation, beta-hydroxybutyrylation, and lactylation, were detected using pan-specific antibodies through Western blot. The samples, consisting of human plasma-derived HSA (pHSA) from six different manufacturers and recombinant HSA (rHSA) expressed in yeast and oryza sativa, underwent detection of types of post-translational modifications. 4D label-free PTMs quantitative proteomic analysis was conducted to detect N-glycosylation and the above-mentioned post-translational modifications in pHSA and rHSA samples, and analyze the differences in modification sites and levels. Through Western blot analysis, all six pHSA and two rHSA samples were positive in the band of albumin (66.5 kDa) for the six post-translational modifications. Further analysis using 4D label-free PTMs quantitative proteomics revealed 25 (29) acetylated, 30 (32) succinylated, 41 (50) malonylated, 15 (23) phosphorylated, 36 (30) beta-hydroxybutyrylated, and 27 (34) lactylated modification sites in pHSA and rHSA samples and no N-glycosylation modification sites. The analysis results identified 1 acetylation (ALB_K160), 2 beta-hydroxybutyrylation (ALB_K569, ALB_K426), 3 crotonylation (ALB_K264, ALB_K581, ALB_K560), and 15 phosphorylation specific modification sites in pHSA, as well as 3 crotonylation (ALB_K560, ALB_K562, ALB_K75), 1 succinylation (ALB_K490), and 23 phosphorylation specific modification sites in rHSA. In pHSA (rHSA), 2 (6) acetylation, 10 (12) succinylation, 0 (9) crotonylation, 1 (9) phosphorylation, 6 (0) beta-hydroxybutyrylation, and 0 (7) lactylation specific modification sites were found. Additionally, in the common modification sites of pHSA and rHSA, pHSA showed up-regulation of amberylation (16:1) and beta-hydroxybutyrylation (12:2) in more sites, and up-regulation of acetylation (7:11), crotonylation (2:11), phosphorylation (1:8), and lactylation (1:14) in less sites compared to rHSA. In clinical treatment, the used pHSA and rHSA in China generally exhibit acetylation, succinylation, crotonylation, phosphorylation, beta-hydroxybutyrylation, and lactylation, and there are differences in the site characteristics and modification levels of these modifications between pHSA and rHSA. Further experimental investigations are needed to explore the impact of post-translational modification differences on the biological function, efficacy, and safety of pHSA and rHSA.

			Action	DRS
	XA01982B1LPST.zip	Other
	XA01982B1LPST_B1_1.raw	Raw
	XA01982B1LPST_B1_2.raw	Raw
	XA01982B1LPST_B1_3.raw	Raw
	XA01982B1LPST_B2_1.raw	Raw

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Phosphorylated proteomics data of protein kinase MoCK2 in Magnaporthe oryzae

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