ArticlePLoS pathogens2008
Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo.
Article in PLoS pathogens, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
122 citing papers in PubMed, 193 citations in OpenAlex.
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- Interplay between proteostasis pathways and innate immune responses inInfection and immunity · 2026Review
- Src-dependent tyrosine-phosphorylation of NM2A has a protective role against bacterial pore-forming toxins.PLoS pathogens · 2026Article
- Intersections between proteostasis and immunity: insights from Caenorhabditis elegans.Disease models & mechanisms · 2026Review
- Vitamin BResearch square · 2025Article
- Bacterial infection elicits theOpen biology · 2025Article
- 'Re-Wilding' an Animal Model With Microbiota Shifts Immunity and Stress Gene Expression During Infection.Molecular ecology · 2025Article
- Unzipping the defense: a comprehensive review on bZIP transcription factors inFrontiers in cellular and infection microbiology · 2025Review
- Resistance to Cry14A family Bacillus thuringiensis crystal proteins in Caenornabditis elegans operates via the nhr-31 transcription factor and vacuolar-type ATPase pathway.PLoS pathogens · 2024Article
- The nematode (Ascaris suum) intestine is a location of synergistic anthelmintic effects of Cry5B and levamisole.PLoS pathogens · 2024Article
- The intricate triangular interaction between protective microbe, pathogen and host determines fitness of the metaorganism.Proceedings. Biological sciences · 2023Article
- Aminopeptidase MNP-1 triggers intestine protease production by activating daf-16 nuclear location to degrade pore-forming toxins in Caenorhabditis elegans.PLoS pathogens · 2023Article
- Article
- Probiotic effects ofFrontiers in physiology · 2023Article
- The endoplasmic reticulum stress-mediated unfolded protein response protects against infection of goat endometrial epithelial cells byVirulence · 2022Article
- A Caenorhabditis elegans nck-1 and filamentous actin-regulating protein pathway mediates a key cellular defense against bacterial pore-forming proteins.PLoS pathogens · 2022Article
- Imaging-associated stress causes divergent phase transitions of RNA-binding proteins in the Caenorhabditis elegans germ line.G3 (Bethesda, Md.) · 2022Article
- Membrane Dynamics and Remodelling in Response to the Action of the Membrane-Damaging Pore-Forming Toxins.The Journal of membrane biology · 2022Review
- The cellular response to plasma membrane disruption for nanomaterial delivery.Nano convergence · 2022Review
- Conserved and Distinct Elements of Phagocytosis in Human andInternational journal of molecular sciences · 2021Review
62 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Pore-forming toxins (PFTs) constitute the single largest class of proteinaceous bacterial virulence factors and are made by many of the most important bacterial pathogens. Host responses to these toxins are complex and poorly understood. We find that the endoplasmic reticulum unfolded protein response (UPR) is activated upon exposure to PFTs both in Caenorhabditis elegans and in mammalian cells. Activation of the UPR is protective in vivo against PFTs since animals that lack either the ire-1-xbp-1 or the atf-6 arms of the UPR are more sensitive to PFT than wild-type animals. The UPR acts directly in the cells targeted by the PFT. Loss of the UPR leads to a normal response against unrelated toxins or a pathogenic bacterium, indicating its PFT-protective role is specific. The p38 mitogen-activated protein (MAPK) kinase pathway has been previously shown to be important for cellular defenses against PFTs. We find here that the UPR is one of the key downstream targets of the p38 MAPK pathway in response to PFT since loss of a functional p38 MAPK pathway leads to a failure of PFT to properly activate the ire-1-xbp-1 arm of the UPR. The UPR-mediated activation and response to PFTs is distinct from the canonical UPR-mediated response to unfolded proteins both in terms of its activation and functional sensitivities. These data demonstrate that the UPR, a fundamental intracellular pathway, can operate in intrinsic cellular defenses against bacterial attack.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.