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Anaerobic respiration of host-derived methionine sulfoxide protects intracellular Salmonella from the phagocyte NADPH oxidase

ABSTRACT: Anaerobic respiration of host-derived methionine sulfoxide protects intracellular Salmonella from the phagocyte NADPH oxidase

PROVIDER: PRJNA1043201 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26893861_1.fastq.gz	Fastqsanger.gz
	SRR26893861_2.fastq.gz	Fastqsanger.gz
	SRR26893862_1.fastq.gz	Fastqsanger.gz
	SRR26893862_2.fastq.gz	Fastqsanger.gz
	SRR26893863_1.fastq.gz	Fastqsanger.gz

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EROS is a selective chaperone regulating the phagocyte NADPH oxidase and purinergic signalling.

Project description:The phagocyte NADPH oxidase is critical for host defence, and EROS (Essential for Reactive Oxygen Species) protein is indispensable for expression of its gp91phox-p22phox heterodimer. EROS deficiency in humans is a recently described cause of chronic granulomatous disease (CGD), but its mechanism of action remains unknown. We show EROS binds the immature 58kDa gp91phox directly prior to glycosylation and heme incorporation, thus preventing its degradation. EROS interacts with the oligosaccharyl transferase complex (OST) present at the endoplasmic reticulum. Inhibition of the OST complex suppresses EROS-mediated stabilisation of the 58kDa, providing insight into the early steps of gp91phox biosynthesis. EROS also regulates the purine receptors P2X7 and P2X1 through direct interactions. Accordingly, lack of EROS results in markedly abnormal P2X7 signalling, inflammasome activation and T cell responses. The loss of both the phagocyte respiratory burst and P2X7 signalling lead to resistance to influenza infection. Our work identifies EROS as the first described highly selective chaperone controlling key proteins in innate and adaptive immunity. It has profound implications for immune physiology, immunodeficiency and gene therapy.

2022-11-30 | PXD025149 | Pride

Anaerobic respiration of host-derived methionine sulfoxide protects intracellular Salmonella from the phagocyte NADPH oxidase

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Anaerobic respiration of host-derived methionine sulfoxide protects intracellular Salmonella from the phagocyte NADPH oxidase.

Project description: Not available

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The role of phagocyte NADPH Oxidase (NOX2) in modulating the antimicrobial and inflammatory functions of mouse neutrophils

Project description:The role of phagocyte NADPH Oxidase (NOX2) in modulating the antimicrobial and inflammatory functions of mouse neutrophils

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Mycobacterium tuberculosis is protected from NADPH oxidase and LC3-associated phagocytosis by the LCP protein CpsA

Project description:Mycobacterium tuberculosis’success as a pathogen comes from itsability to evade degradation by macrophages. Normally macro-phages clear microorganisms that activate pathogen-recognitionreceptors (PRRs) through a lysosomal-trafficking pathway called“LC3-associated phagocytosis”(LAP). AlthoughM.tuberculosisac-tivates numerous PRRs, for reasons that are poorly understoodLAP does not substantially contribute toM.tuberculosiscontrol.LAP depends upon reactive oxygen species (ROS) generated byNADPH oxidase, butM.tuberculosisfails to generate a robustoxidative response. Here, we show that CpsA, a LytR-CpsA-Psr(LCP) domain-containing protein, is required forM.tuberculosisto evade killing by NADPH oxidase and LAP. Unlike phagosomescontaining wild-type bacilli, phagosomes containing theΔcpsAmutant recruited NADPH oxidase, produced ROS, associated withLC3, and matured into antibacterial lysosomes. Moreover, CpsAwas sufficient to impair NADPH oxidase recruitment to fungal par-ticles that are normally cleared by LAP. Intracellular survival of theΔcpsAmutant was largely restored in macrophages missing LAPcomponents (Nox2,Rubicon,Beclin,Atg5,Atg7,orAtg16L1) butnot in macrophages defective in a related, canonical autophagypathway (Atg14,Ulk1,orcGAS). TheΔcpsAmutant was highlyimpaired in vivo, and its growth was partially restored in micedeficient in NADPH oxidase,Atg5,orAtg7, demonstrating thatCpsA makes a significant contribution to the resistance ofM.tu-berculosisto NADPH oxidase and LC3 trafficking in vivo. Overall,our findings reveal an essential role of CpsA in innate immuneevasion and suggest that LCP proteins have functions beyond theirpreviously known role in cell-wall metabolism.

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NADPH Oxidase 4 and Metabolic Stress in Dahl Salt-Sensitive Rat Kidneys

Project description:This study investigated how redox regulation influences renal metabolic reprogramming induced by high salt (HS) intake, by comparing Dahl salt-sensitive (SS) rats and SS rats deficient in NADPH oxidase 4 (SSNOX4⁻/⁻). In SS rats, HS intake upregulated glutaminase and increased glutamate consumption, reflecting a shift toward glutamine-driven metabolism, inefficient oxygen utilization, and elevated ROS. In contrast, SSNOX4⁻/⁻ rats exhibited intrinsically higher NO production and favored fatty acid oxidation (FAO), promoting more efficient oxygen. Notably, renal lactate release was observed exclusively in SSNOX4⁻/⁻ rats following HS intake, despite no glycolytic gene upregulation, suggesting increased lactate production due to a substrate shift, possibly toward enhanced FAO. Furthermore, SSNOX4⁻/⁻ rats did not exhibit the salt-induced augmentation of amino acid metabolism seen in SS rats, indicating a protein-sparing metabolic adaptation. Together, these findings reveal a distinct metabolic reprogramming in SSNOX4⁻/⁻ rats that enhances energy efficiency and contributes to renal protection under HS conditions.

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