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The pore-forming apolipoprotein APOL7C drives phagosomal rupture and antigen cross-presentation by dendritic cells

ABSTRACT: The pore-forming apolipoprotein APOL7C drives phagosomal rupture and antigen cross-presentation by dendritic cells

PROVIDER: PRJNA1165795 | ENA |

REPOSITORIES: ENA

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The pore-forming apolipoprotein APOL7C drives phagosomal rupture and antigen cross-presentation by dendritic cells

Project description:Conventional dendritic cells (cDCs) generate protective cytotoxic T lymphocyte (CTL) responses against pathogens and tumours. This is achieved through a process known as cross-presentation (XP) and, despite its obvious biological importance, the mechanism(s) driving XP remain unclear. Here, we show that a cDC-specific pore-forming protein called apolipoprotein L 7C (APOL7C) is upregulated in response to innate immune stimuli and is recruited to phagosomes. Strikingly, its association with phagosomes leads to phagosomal rupture. This allows for the escape of engulfed antigens to the cytosol where they can be processed via the endogenous MHC class I antigen processing pathway. Accordingly, mice deficient in APOL7C do not efficiently prime CD8+ T cells in response to immunization with bead-bound and cell-associated antigens. Altogether, our data indicate the presence of dedicated apolipoproteins that mediate the delivery of phagocytosed proteins to the cytosol of activated cDCs to facilitate XP.

2024-09-25 | GSE276376 | GEO

The pore-forming apolipoprotein APOL7C drives phagosomal rupture and antigen cross-presentation by dendritic cells

Project description:The pore-forming apolipoprotein APOL7C drives phagosomal rupture and antigen cross-presentation by dendritic cells

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The pore-forming apolipoprotein APOL7C drives phagosomal rupture and antigen cross-presentation by dendritic cells

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Bacterial pore-forming toxin pneumolysin drives pathogenicity through host extracellular vesicles released during infection

Project description:In this study, we characterized the proteomic composition of extracellular vesicles released from human THP-1 monocytes challenged with the pneumococcal pore-forming toxin, pneumolysin. We found that the vesicles shed from pneumolysin challenged cells are selectively enriched in key inflammatory host proteins relative to vesicles from untreated cells.

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Listeria monocytogenes induces T cell receptor unresponsiveness via its pore-forming toxin listeriolysin O

Project description:The success of many pathogens relies on their ability to circumvent the innate and adaptive immune defenses. How bacterial pathogens subvert host responses is not clear. Cholesterol-dependent cytolysins (CDCs) represent an expansive family of homologous pore-forming toxins produced by more than 20 Gram-positive bacterial species. Here we show that listeriolysin O (LLO), a prototype CDC produced by Listeria monocytogenes, inhibits antigen receptor-induced T cell proliferation. In vivo proliferation of OT II T cells was highly diminished in the presence of wild type but not the LLO-deficient bacteria. T cells pre-exposed to LLO ex vivo were also impaired in proliferation upon TCR activation in vivo and in vitro. Our results suggest that LLO-induced T cell unresponsiveness is due to the sub-threshold activation of T cells via the induction of a calcium-NFAT dependent transcriptional program that drives the expression of negative regulators of TCR signaling. Keywords: Listerilysin O, Ionomycin, 3 hours stimulation Pooled primary CD4+ T cells isolated from spleen and mesenteric lymph nodes were incubated in either control (Ctrl) medium or medium containing 0.25 ug/ml listeriolysin O (LLO) or 1 uM Ionomycin (Iono) for 3 hours. Thereafter, cells were washed and RNA was prepared.

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Listeria monocytogenes induces T cell receptor unresponsiveness via its pore-forming toxin listeriolysin O

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HLH-30/TFEB-mediated autophagy functions in a cell-autonomous manner for epithelium intrinsic cellular defense against bacterial pore-forming toxin in C. elegans

Project description:Autophagy is an evolutionarily conserved intracellular system that maintains cellular homeostasis by degrading and recycling damaged cellular components. The transcription factor HLH-30/TFEB-mediated autophagy has been reported to regulate tolerance to bacterial infection, but less is known about the bona fide bacterial effector that activates HLH-30 and autophagy. Here, we unveil that bacterial membrane pore-forming toxin (PFT) induces autophagy through an HLH-30-dependent manner in Caenorhabditis elegans. Moreover, autophagy controls the susceptibility of animals to PFT toxicity through xenophagic degradation of PFT and repair of membrane-pore cell-autonomously in the PFT-targeted intestinal cells in C. elegans. These results demonstrate that autophagic pathways and autophagy are induced partly at the transcriptional level through HLH-30 activation and are required to protect metazoan upon PFT intoxication. Together, our data show a new and powerful connection between HLH-30-mediated autophagy and epithelium intrinsic cellular defense against the single most common mode of bacterial attack in vivo.

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Alternative splicing induced by bacterial pore-forming toxins sharpens CIRBP-mediated cell response to Listeria infection

Project description:Alternative splicing induced by bacterial pore-forming toxins sharpens CIRBP-mediated cell response to Listeria infection

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