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Proteomic data of protein kinase MoCK2 in Magnaporthe oryzae

ABSTRACT: Through proteomic analysis comparing the abundance changes between knockout mutants of the two regulatory subunits of protein kinase MoCK2 and the wild-type Ku80 in Magnaporthe oryzae, this study reveals the underlying regulatory mechanisms by which the absence of MoCK2 leads to loss of pathogenicity in the fungus. It provides theoretical research directions for subsequent investigations into the pathogenic mechanisms.

INSTRUMENT(S):

ORGANISM(S): Pyricularia Oryzae 70-15

TISSUE(S): Mycelium

SUBMITTER: Lianhu Zhang

LAB HEAD: Lianhu Zhang

PROVIDER: PXD066250 | 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.

			Action	DRS
	XA01982B1LQ.zip	Other
	XA01982B1LQ_B1_1.raw	Raw
	XA01982B1LQ_B1_2.raw	Raw
	XA01982B1LQ_B1_3.raw	Raw
	XA01982B1LQ_B2_1.raw	Raw

Dataset Information

Proteomic data of protein kinase MoCK2 in Magnaporthe oryzae

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