ArticleJournal of bacteriology2003
Requirement of the Listeria monocytogenes broad-range phospholipase PC-PLC during infection of human epithelial cells.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 141 citations in OpenAlex.
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- Novel amino acid residues in listerolysin O drive phagosome escape and pathogenicity inVirulence · 2025Article
- Unravelling the genomic landscape of Acinetobacter baumannii: deep dive into virulence factors, resistance elements, and evolutionary adaptations.Molecular genetics and genomics : MGG · 2025Article
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- Pathogenic rickettsiae encode a secreted lipase that facilitates intracytosolic colonization in host cells.PloS one · 2025Article
- Bacterial aggregation facilitates internalin-mediated invasion ofFrontiers in cellular and infection microbiology · 2024Article
- Structural basis for the unique molecular properties of broad-range phospholipase C from Listeria monocytogenes.Nature communications · 2023Article
- Comparison of genetic variations between high- and low-riskFrontiers in microbiology · 2023Article
- Review
- A patatin-like phospholipase mediates Rickettsia parkeri escape from host membranes.Nature communications · 2022Article
- The TFAMoplex-Conversion of the Mitochondrial Transcription Factor A into a DNA Transfection Agent.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase.FEBS open bio · 2021Review
- Entropy-driven translocation of disordered proteins through the Gram-positive bacterial cell wall.Nature microbiology · 2021Article
- Review
- Characterization of the pathogenesis and immune response to Listeria monocytogenes strains isolated from a sustained national outbreak.Scientific reports · 2019Article
- An ATG16L1-dependent pathway promotes plasma membrane repair and limits Listeria monocytogenes cell-to-cell spread.Nature microbiology · 2018Article
- Principles of intracellular bacterial pathogen spread from cell to cell.PLoS pathogens · 2018Review
- Review
- Pathways of host cell exit by intracellular pathogens.Microbial cell (Graz, Austria) · 2018Review
6 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In this study, we investigated the requirement of the Listeria monocytogenes broad-range phospholipase C (PC-PLC) during infection of human epithelial cells. L. monocytogenes is a facultative intracellular bacterial pathogen of humans and a variety of animal species. After entering a host cell, L. monocytogenes is initially surrounded by a membrane-bound vacuole. Bacteria promote their escape from this vacuole, grow within the host cell cytosol, and spread from cell to cell via actin-based motility. Most infection studies with L. monocytogenes have been performed with mouse cells or an in vivo mouse model of infection. In all mouse-derived cells tested, the pore-forming cytolysin listeriolysin O (LLO) is absolutely required for lysis of primary vacuoles formed during host cell entry. However, L. monocytogenes can escape from primary vacuoles in the absence of LLO during infection of human epithelial cell lines Henle 407, HEp-2, and HeLa. Previous studies have shown that the broad-range phospholipase C, PC-PLC, promotes lysis of Henle 407 cell primary vacuoles in the absence of LLO. Here, we have shown that PC-PLC is also required for lysis of HEp-2 and HeLa cell primary vacuoles in the absence of LLO expression. Furthermore, our results indicated that the amount of PC-PLC activity is critical for the efficiency of vacuolar lysis. In an LLO-negative derivative of L. monocytogenes strain 10403S, expression of PC-PLC has to increase before or upon entry into human epithelial cells, compared to expression in broth culture, to allow bacterial escape from primary vacuoles. Using a system for inducible PC-PLC expression in L. monocytogenes, we provide evidence that phospholipase activity can be increased by elevated expression of PC-PLC or Mpl, the enzyme required for proteolytic activation of PC-PLC. Lastly, by using the inducible PC-PLC expression system, we demonstrate that, in the absence of LLO, PC-PLC activity is not only required for lysis of primary vacuoles in human epithelial cells but is also necessary for efficient cell-to-cell spread. We speculate that the additional requirement for PC-PLC activity is for lysis of secondary double-membrane vacuoles formed during cell-to-cell spread.
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