ArticleJournal of microbiology (Seoul, Korea)2014
VvpM, an extracellular metalloprotease of Vibrio vulnificus, induces apoptotic death of human cells.
Article in Journal of microbiology (Seoul, Korea), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Direct and indirect effects of pathogenic bacteria on the integrity of intestinal barrier.Therapeutic advances in gastroenterology · 2023Review
- Vibrio vulnificus PlpA facilitates necrotic host cell death induced by the pore forming MARTX toxin.Journal of microbiology (Seoul, Korea) · 2022Article
- The DNA binding domain of the Vibrio vulnificus SmcR transcription factor is flexible and binds diverse DNA sequences.Nucleic acids research · 2021Article
- The role of Vibrio vulnificus virulence factors and regulators in its infection-induced sepsis.Folia microbiologica · 2020Review
- Melatonin restores Muc2 depletion induced by V. vulnificus VvpM via melatonin receptor 2 coupling with Gαq.Journal of biomedical science · 2020Article
- The extracellular proteases produced by Vibrio parahaemolyticus.World journal of microbiology & biotechnology · 2018Review
- Repression of VvpM Protease Expression by Quorum Sensing and the cAMP-cAMP Receptor Protein Complex in Vibrio vulnificus.Journal of bacteriology · 2018Article
- The hydrogen peroxide hypersensitivity of OxyR2 inThe Journal of biological chemistry · 2017Article
- Crystal Structure of the Regulatory Domain of AphB fromMolecules and cells · 2017Article
- Review
- AFrontiers in cellular and infection microbiology · 2017Article
- The Makes Caterpillars Floppy (MCF)-Like Domain of Vibrio vulnificus Induces Mitochondrion-Mediated Apoptosis.Infection and immunity · 2015Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A pathogenic bacterium, Vibrio vulnificus produces various extracellular proteases including the elastolytic metalloprotease, VvpE. In silico analysis of its genome revealed a VvpE-homologous protease, VvpM whose proteolytic activity was abolished by specific inhibitors against metalloproteases. To investigate whether this newly identified protease has pathogenic role in host interaction in addition to proteolytic role, human cell lines were incubated with recombinant VvpM (rVvpM). rVvpM-challenged cells showed typical morphological changes found in cells under apoptosis. Apoptotic cell death was further evidenced by estimating the Annexin V-stained cells, whose proportions were dependent upon the concentrations of rVvpM treated to human cells. To elucidate the signaling pathway for VvpM-induced apoptosis, three MAPKs were tested if their activation were mediated by rVvpM. ERK1/2 was phosphorylated by treatment of rVvpM and rVvpM-induced cell death was blocked by a specific inhibitor against ERK1/2. In rVvpM-treated cells, the cytosolic levels of cytochrome c were increased in a VvpM concentration-dependent manner, while the levels of cytochrome c in mitochondria were decreased. Cell deaths were accompanied by apparent cleavages of procaspases-9 and -3 to the active caspases-9 and -3, respectively. Therefore, this study demonstrates that an extracellular metalloprotease of V. vulnificus, VvpM induces apoptosis of human cells via a pathway consisting of ERK activation, cytochrome c release, and then activation of caspases-9 and -3.
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