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HERPES SIMPLEX VIRUS TYPE 1 IMPAIRS DENDRITIC CELL FUNCTION BY REMODELLING NEUTRAL LIPID METABOLISM AND INDUCING LIPID DROPLET ACCUMULATION

ABSTRACT: HERPES SIMPLEX VIRUS TYPE 1 IMPAIRS DENDRITIC CELL FUNCTION BY REMODELLING NEUTRAL LIPID METABOLISM AND INDUCING LIPID DROPLET ACCUMULATION

PROVIDER: PRJNA998087 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25409445_1.fastq.gz	Fastqsanger.gz
	SRR25409445_2.fastq.gz	Fastqsanger.gz
	SRR25409446_1.fastq.gz	Fastqsanger.gz
	SRR25409446_2.fastq.gz	Fastqsanger.gz
	SRR25409447_1.fastq.gz	Fastqsanger.gz

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HERPES SIMPLEX VIRUS TYPE 1 IMPAIRS DENDRITIC CELL FUNCTION BY REMODELLING NEUTRAL LIPID METABOLISM AND INDUCING LIPID DROPLET ACCUMULATION

Project description:Herpes simplex virus type 1 (HSV-1) infects dendritic cells (DCs), professional antigen-presenting cells that initiate and regulate host antiviral responses. HSV-1 infects DCs limiting their maturation, migration to draining lymph nodes and T cell activation capacity, ultimately promotes their apoptosis. Here, we investigated the impact of HSV-1 infection over neutral lipid metabolism in DCs and their function. We found that HSV-1 significantly alters neutral lipid metabolism in infected DCs and promotes LD accumulation. Pharmacological inhibition of cholesterol ester synthesis, or fatty acid transporter proteins in infected DCs reduced LD accumulation and viral replication, enhanced DC viability and DC migration to draining lymph nodes and promoted DC priming of virus-specific CD8+ T cells. These findings highlight the role of neutral lipid metabolism in HSV-1-infected DCs and its impact over host immunity against this virus, underscoring lipid metabolism in DCs as a potential therapeutical target for triggering antiviral immunity against HSV-1.

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HERPES SIMPLEX VIRUS TYPE 1 IMPAIRS DENDRITIC CELL FUNCTION BY REMODELLING NEUTRAL LIPID METABOLISM AND INDUCING LIPID DROPLET ACCUMULATION

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Altered hepatic lipid droplet morphology and lipid metabolism in fasted Plin2 null mice

Project description:Perilipin 2 (Plin2) binds to the surface of hepatic lipid droplets (LDs) with expression levels that correlate with triacylglyceride (TAG) content. We investigated if Plin2 is important for hepatic LD storage in fasted or high-fat diet-induced obese Plin2+/+ and Plin2-/- mice. Plin2-/- mice had comparable body weights, metabolic phenotype, glucose tolerance, and circulating TAG and total cholesterol levels compared to Plin2+/+ mice, regardless of the dietary regime. Both fasted and high-fat fed Plin2-/- mice stored reduced levels of hepatic TAG compared to Plin2+/+ mice. Fasted Plin2-/- mice stored fewer, but larger hepatic lipid droplets compared to Plin2+/+ mice. Detailed hepatic lipid analysis showed substantial reductions in accumulated TAG species in fasted Plin2-/- mice compared to Plin2+/+ mice, whereas cholesteryl esters and phosphatidylcholines were increased. RNA sequencing revealed minor differences in hepatic gene expression between fed Plin2+/+ and Plin2-/- mice, in contrast to marked differences in gene expression between fasted Plin2+/+ and Plin2-/- mice. Our findings demonstrate that Plin2 is required to regulate hepatic lipid droplet size and storage of neutral lipid species in the fasted state, while its role in obesity-induced steatosis is less clear.

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RNA-seq of lipid droplet-low and lipid droplet-rich microglia isolated from the hippocampi of aged mice

Project description:Sequencing data related to the manuscript entitled, "Lipid droplet accumulating microglia represent a dysfunctional and pro-inflammatory state in the aging brain".

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Arabidopsis LDIP is an LDAP-interacting protein that influences lipid droplet biogenesis and neutral lipid homeostasis in both leaves and seeds

Project description:Cytoplasmic lipid droplets (LDs) are found in all types of plant cells where they are derived from the endoplasmic reticulum (ER) and function as a repository for neutral lipids, as well as serving in lipid remodelling and signalling. However, the mechanisms underlying the formation and functioning of plant LDs, particularly in non-seed tissues, are relatively unknown. Previously, we showed that the LD-Associated Proteins (LDAPs) are a family of plant-specific, LD surface-associated coat proteins that are required for proper LD biogenesis and neutral lipid homeostasis in vegetative tissues. Here, we screened a yeast two-hybrid library using Arabidopsis LDAP3 as ‘bait’ in an effort to identify other novel LD protein constituents. One of the candidate LDAP3-interacting proteins was Arabidopsis At5g16550, which is a plant-specific protein of unknown function that we termed LDIP (LDAP-interacting protein). Using a combination of biochemical and cellular approaches, we show that LDIP targets specifically to the LD surface, contains a discrete amphipathic -helical targeting sequence, and participates in both homotypic and heterotypic associations with itself and LDAP3, respectively. Analysis of LDIP T-DNA knockdown and knockout mutants showed a decrease in LD abundance and increase in variability of LD size in leaves, with concomitant increases in total neutral lipid content. Similar phenotypes were observed in plant seeds, which showed enlarged LDs and increases in total seed oil amounts. Collectively, these data identify LDIP as a new player in LD biogenesis in plants that modulates both LD size and cellular neutral lipid homeostasis. Potential mechanisms of LDIP activity are discussed.

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The lipid droplet protein DHRS3 is a regulator of melanoma cell state

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