Regular ArticleNeurotoxicity of Pneumolysin, a Major Pneumococcal Virulence Factor, Involves Calcium Influx and Depends on Activation of p38 Mitogen-Activated Protein Kinase☆
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Ca<sup>2+</sup>-calmodulin signalling at the host-pathogen interface
2023, Current Opinion in MicrobiologyBacillus thuringiensis cry toxin triggers autophagy activity that may enhance cell death
2021, Pesticide Biochemistry and PhysiologyCitation Excerpt :In our experiments, silencing of JNK expression or inhibition of JNK activity, resulted in lower mortality of the cells, suggesting that JNK signaling pathway may also be participating in inducing the cell death response after treatment of cells with the Cry toxins. These data are related to the Streptococcus pneumoniae pneumolysin (PLY) that mediated cytotoxicity in human neuroblastoma cells (Stringaris et al., 2002). In that report the blocking of p38 kinase activity also reduces PLY-mediated cytotoxicity in the neuroblastoma cells, suggesting that MAPK activation during intoxication with pore forming toxins may enhance cell death (Stringaris et al., 2002).
Vibrio vulnificus cytolysin induces inflammatory responses in RAW264.7 macrophages through calcium signaling and causes inflammation in vivo
2019, Microbial PathogenesisCitation Excerpt :In this report, we show that VVC induces an influx of Ca2+ to activate NF-κB, MAPKs, and AKT signaling pathways. Previous research shows that mobilization of Ca2+ leads to JNK, p38, ERK1/2, and AKT phosphorylation [20–23], and that p65 can be activated by p-ERK1/2 [39] and p-AKT [40]. The NF-κB and p38 MAPK signal transduction pathways play important roles in stress responses such as inflammation, and may be the main cause of pro-inflammatory cytokines production induced by VVC.
Pneumolysin induces cellular senescence by increasing ROS production and activation of MAPK/NF-κB signal pathway in glial cells
2017, ToxiconCitation Excerpt :Collectively, our results indicate that PLY triggers senescence of microglial cells through ROS-mediated MAPK activation. It should be noted that although other kinase pathways were not examined, p38 MAPK was activated in PLY-treated neuroblastoma (Stringaris et al., 2002). This discrepancy possibly arose from the different cell type used in experiment.
Toxicity of Cry1A toxins from Bacillus thuringiensis to CF1 cells does not involve activation of adenylate cyclase/PKA signaling pathway
2017, Insect Biochemistry and Molecular BiologyCitation Excerpt :This model was described in a cell line of Trichoplusia ni named H5 cells (T.ni Hi5) that became sensitive to Cry1Ab since it was transfected with the Manduca sexta cadherin receptor gene (Zhang et al., 2006). On the other side a defense response to PFTs involving the activation of mitogen activated kinases such as MAPK p38 and JNK, has been observed in different cells after intoxication with low doses of several PFTs produced by different bacteria such as streptolysin O (SLO) from Streptococcus pyogenes (Stassen et al., 2003), pneumolysin from Streptococcus pneumonia (Stringaris et al., 2002); alpha toxin from Staphylococcus aureus (Husmann et al., 2006); aerolysin from Aeromonas hydrophila (Huffman et al., 2004) including different Bacillus thruringiensis toxins such as Cry1Ab, Cry3Aa, Cry11Aa, and Cry5B, which are toxic to different insect orders (Lepidoptera, Coleoptera and Diptera) and nematodes, respectively (Huffman et al., 2004; Cancino-Rodezno et al., 2010; Oppert et al., 2012). Silencing of the p38 gene by RNAi or mutations in the p38 or jnk genes resulted in hypersensitivity to these toxins, showing that p38 and JNK are involved in the defense response to PFTs (Huffman et al., 2004; Cancino-Rodezno et al., 2010; Oppert et al., 2012).
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Part of these data has been presented as a poster at the 54th Annual Meeting of the American Academy of Neurology in Denver Colorado.
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These authors contributed equally to this work.
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To whom correspondence should be addressed to Dr. Roland Nau, Department of Neurology, Georg-August-University, Robert-Koch-Strasse 40, 37075 Göttingen, Germany. Fax: ++49 551 398405. E-mail: [email protected].