Dataset Information

Label-free quantitative proteomic analysis of Mycobacterium avium hominissuis

ABSTRACT: The objective of this study is to investigate the protein expression level difference between Mycobacterium avium hominissuis wild type strain MAH-104 , its mutant 21m (gene lysX (MAV_3128) mutated - Lysyl tRNA synthetase) and the complemented strain 21c (MAV_3128comp) using liquid chromatography-mass spectrometry (LC/MS) based label free quantitative proteomics analysis.

INSTRUMENT(S):

ORGANISM(S): Mycobacterium Avium Complex Mycobacterium Avium Subsp. Hominissuis

SUBMITTER: Jayaseelan Murugaiyan

LAB HEAD: Jayaseelan Murugaiyan

PROVIDER: PXD006470 | Pride | 2018-02-26

REPOSITORIES: Pride

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Publications

Proteome Analysis of a M. avium Mutant Exposes a Novel Role of the Bifunctional Protein LysX in the Regulation of Metabolic Activity.

Kirubakar Greana G Murugaiyan Jayaseelan J Schaudinn Christoph C Dematheis Flavia F Holland Gudrun G Eravci Murat M Weise Christoph C Roesler Uwe U Lewin Astrid A

The Journal of infectious diseases 20180601 2

Lysyl-phosphatidylglycerol is one of the components of the mycobacterial membrane that contributes to the resistance to cationic antimicrobial peptides, a host-induced frontline defense against invading pathogens. Its production is catalyzed by LysX, a bifunctional protein with lysyl transferase and lysyl transfer RNA synthetase activity. Comparative proteome analysis of a lysX mutant of Mycobacterium avium strain 104 and the wild type indicated that the lysX mutant strain undergoes a transition ...[more]

PMID: 29471363

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Project description:Ineffective hematopoiesis is a hallmark of myelodysplastic syndromes (MDS). Hematopoietic alterations in MDS patients strictly correlate with microenvironment dysfunctions, eventually affecting also the mesenchymal stromal cells (MSCs) compartment. Stromal cells are indeed epigenetically reprogrammed to cooperate with leukemic cells and propagate the disease as "tumor unit"; therefore, changes on MSCs epigenetic profile might contribute to the hematopoietic perturbations typical of MDS. Here, we unveil that the histone variant macroH2A1 (mH2A1) regulates the crosstalk between epigenetics and inflammation in MDS-MSCs, potentially affecting their hematopoietic support ability. We show that the mH2A1 splicing isoform mH2A1.1 accumulates in MDS-MSCs, correlating with the expression of the Toll-like receptor 4 (TLR4), an important pro-tumor activator of MSC phenotype associated to a pro-inflammatory behavior. MH2A1.1-TLR4 axis was further investigated in HS-5 stromal cells after ectopic mH2A1.1 overexpression (mH2A1.1-OE). Proteomic data confirmed the activation of a pro-inflammatory signature associated to TLR4 and nuclear factor kappa B (NFkB) activation. Moreover, mH2A1.1-OE proteomic profile identified several upregulated proteins associated to DNA and histones hypermethylation, including S-adenosylhomocysteine hydrolase, a strong inhibitor of DNA methyltransferase and of the methyl donor S-adenosyl-methionine (SAM). HPLC analysis confirmed higher SAM/SAH ratio along with a metabolic reprogramming. Interestingly, an increased LDHA nuclear localization was detected both in mH2A1.1-OE cells and MDS-MSCs, probably depending on MSC inflammatory phenotype. Finally, coculturing healthy mH2A1-OE MSCs with CD34+ cells, we found a significant reduction in the number of CD34+ cells, which was reflected in a decreased number of colony forming units (CFU -Cs). These results suggest a key role of mH2A1.1 in driving the crosstalk between epigenetic signaling, inflammation and cell metabolism networks in MDS-MSCs.

			Action	DRS
	MSrawfiledetails.xlsx	Xlsx
	MaxQuantResultfile.zip	Other
	P1C_01.raw	Raw
	P1C_02.raw	Raw
	P1C_03.raw	Raw