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ProteomicsShort-term remodeling of the host epithelial cell proteome by the listeriolysin O pore-forming toxin
Bacterial pathogens use various strategies to interfere with host cell functions. Among these strategies, bacteria induce transcriptional changes, in order to modify the set of proteins synthetized by the host cell, or target pre-existing proteins by modulating their post-translational modifications...
ORGANISM(S): Homo sapiens (Human) 
2018-05-17 | PXD009339 | Pride
Pore-forming toxin Listeriolysin o Bacterial infection Listeria 
TranscriptomicsTranscription profiling of human HeLa cells treated with major listerial toxin listeriolysin
Upon infection, pathogens reprogram host gene expression. In eukaryotic cells, genetic reprogramming is induced by the concerted activation/repression of transcription factors and various histone modifications that control DNA accessibility in chromatin. We report here that the bacterial pathogen, ...
ORGANISM(S): Homo sapiens 
2008-04-01 | E-MEXP-1078 | biostudies-arrayexpress
ProteomicsBacterial pore-forming toxins remodel the host epithelial cell proteome
Bacterial pathogens use various strategies to interfere with host cell functions. Among these strategies, bacteria induce transcriptional changes, in order to modify the set of proteins synthetized by the host cell, or target pre-existing proteins by modulating their post-translational modifications...
ORGANISM(S): Homo sapiens (Human) 
2018-11-07 | PXD006900 | Pride
Listeria infection Pore-forming toxin Silac Listeriolysin o 
ProteomicsA pore-forming toxin initiates ABI1 complex switching to promote bacterial cell-to-cell spread
Listeria monocytogenes (Lm), a prototypical intracellular bacterial pathogen, expresses ActA to initiate ARP2/3-mediated actin-based motility in the cytosol of host cells. Motile bacteria generate Lm-containing protrusions at the cell surface, facilitating direct cell-to-cell spread and disseminatio...
ORGANISM(S): Homo sapiens (Human) 
2026-06-15 | PXD074581 | Pride
Cell-to-cell spread Listeria Infectious diseases Ip-ms 
TranscriptomicsListeria monocytogenes induces T cell receptor unresponsiveness via its pore-forming toxin listeriolysin O
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 G...
ORGANISM(S): Mus musculus 
2010-07-29 | E-GEOD-19337 | biostudies-arrayexpress
ProteomicsBacterial pore-forming toxins remodel the host epithelial cell proteome
Bacterial pathogens use various strategies to interfere with host cell functions. Among these strategies, bacteria induce transcriptional changes, in order to modify the set of proteins synthetized by the host cell, or target pre-existing proteins by modulating their post-translational modifications...
ORGANISM(S): Homo sapiens (Human) 
2018-11-07 | PXD006996 | Pride
Listeria Infection Listeriolysin o 
TranscriptomicsConserved immune regulator HLH-30/TFEB couples pore-forming toxin damage sensing to intestine homeostasis via TTC38 signal orchestrator
Effector-triggered immunity (ETI) safeguards intestinal epithelial cells (IECs) by surveilling bacterial virulence effectors and effector-induced cellular stress, such as plasma membrane damage induced by pore-forming toxins (PFTs). However, the knowledge about ETI regulators in maintaining IEC home...
ORGANISM(S): Caenorhabditis elegans 
2025-11-11 | E-MTAB-15698 | biostudies-arrayexpress
UnknownMembrane-Pore Forming Characteristics of the Bordetella pertussis CyaA-Hemolysin Domain.
Not available
S-EPMC4448159 | biostudies-literature
ProteomicsBacterial pore-forming toxin pneumolysin drives pathogenicity through host extracellular vesicles released during infection
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 hos...
ORGANISM(S): Homo sapiens (Human) 
2024-07-31 | PXD052436 | Pride
Human Monocytes Pneumolysin challenge Inflammation Streptococcus pneumoniae Lc-ms Exosome cargo 
UnknownCurcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin Vibrio cholerae Cytolysin.
Not available
S-EPMC8818996 | biostudies-literature
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