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Chromatin Landscape of Macrophages Following Helminth Enzyme Exposure Targeting Prostaglandin Synthesis

ABSTRACT: Chromatin Landscape of Macrophages Following Helminth Enzyme Exposure Targeting Prostaglandin Synthesis

PROVIDER: PRJNA1081279 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28116616.fastq.gz	Fastqsanger.gz
	SRR28116617.fastq.gz	Fastqsanger.gz
	SRR28116618.fastq.gz	Fastqsanger.gz
	SRR28116619.fastq.gz	Fastqsanger.gz
	SRR28116620.fastq.gz	Fastqsanger.gz

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Gene expression profile of Macrophages Following Helminth Enzyme Exposure Targeting Prostaglandin Synthesis

Project description:Gene expression profile of Macrophages Following Helminth Enzyme Exposure Targeting Prostaglandin Synthesis

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Chromatin Landscape of Macrophages Following Helminth Enzyme Exposure Targeting Prostaglandin Synthesis

Project description:The molecular mechanisms by which worm parasites evade host immunity are incompletely understood. In a mouse model of chronic intestinal helminth infection, we identify helminthic glutamate dehydrogenase (heGDH) as an essential factor for parasite chronicity by using antibody mediated neutralization or treatment with exogenous recombinant heGDH. Macrophages efficiently internalize heGDH and represent a major target of the enzyme in vivo. Combining RNA-seq, ChIP-seq, targeted lipidomics and inhibitor studies, we identify prostaglandin E2 (PGE2) as a major immune regulatory mechanism of heGDH. The induction of PGE2 and further immune regulatory factors (IL-12 family cytokines, IDO1) by heGDH depended on the p300-mediated acetylation of histones. While the enzyme’s catalytic activity was dispensable for key immune regulatory functions, an N-terminal handle-like structure distinct from mammalian GDHs may confer interaction of heGDH with its targets (CD64, GPNMB), identified via proteomics. Thus, helminths employ a ubiquitous metabolic enzyme to epigenetically target macrophages and establish chronicity.

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Gene expression profile of Macrophages Following Helminth Enzyme Exposure Targeting Prostaglandin Synthesis

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Project description:Prostaglandin H synthases (PGHSs) are N-glycosylated membrane proteins that catalyse the committed step in prostaglandin synthesis. Unlike PGHS-2, the production of recombinant PGHS-1 in non-mammalian expression systems is complicated. The majority of the heterologous enzyme is inactive due to misfolding. N-glycosylation is proposed to be obligatory for the correct folding of mammalian PGHSs. In this study, human PGHS-1 and -2 (hPGHS-1 and -2) were expressed in the yeast Pichia pastoris, and the N-glycosylation patterns of the purified recombinant proteins were characterised using nano-LC/MS/MS. Recombinant hPGHS-2 was catalytically active, whereas hPGHS-1 was inactive. Unexpectedly, the accumulation of non-glycosylated hPGHS-1 was not observed in the crude lysate of the yeast cells. In addition, the purified hPGHS isoforms exhibited similar N-glycosylation site occupancy. The results indicate that there are more complex grounds for the inactivity of the recombinant hPGHS-1 produced in yeast.

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