ArticleJournal of bacteriology2011
Posttranslocation chaperone PrsA2 regulates the maturation and secretion of Listeria monocytogenes proprotein virulence factors.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 33 citations in OpenAlex.
- The serine-rich C-terminal tail of the Listeria monocytogenes secretion chaperone PrsA2 is critical for bacterial virulence and resistance to cell-wall active antibiotics.PLoS pathogens · 2026Article
- The roles of theJournal of bacteriology · 2026Article
- An insight into the role of branched-chain α-keto acid dehydrogenase (BKD) complex in branched-chain fatty acid biosynthesis and virulence ofJournal of bacteriology · 2024Article
- The chaperone PrsA2 regulates the secretion, stability, and folding of listeriolysin O duringmBio · 2024Article
- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
- Article
- Comparative Genomics Reveal the Utilization Ability of Variable Carbohydrates as Key Genetic Features ofPathogens (Basel, Switzerland) · 2022Article
- Listeria monocytogenes two component system PieRS regulates secretion chaperones PrsA1 and PrsA2 and enhances bacterial translocation across the intestine.Molecular microbiology · 2022Article
- Listeria innocua isolated from diseased ruminants harbour minor virulence genes of L. monocytogenes.Veterinary medicine and science · 2022Article
- Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability ofApplied and environmental microbiology · 2020Article
- Article
- PrsA2 (CD630_35000) ofFrontiers in microbiology · 2018Article
- Listeriolysin O: from bazooka to Swiss army knife.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Secretion Chaperones PrsA2 and HtrA Are Required for Listeria monocytogenes Replication following Intracellular Induction of Virulence Factor Secretion.Infection and immunity · 2016Article
- A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence.Molecular microbiology · 2016Article
- Identification of Conserved and Species-Specific Functions of the Listeria monocytogenes PrsA2 Secretion Chaperone.Infection and immunity · 2015Article
- Listeria monocytogenes is resistant to lysozyme through the regulation, not the acquisition, of cell wall-modifying enzymes.Journal of bacteriology · 2014Article
- Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.Microbiology and molecular biology reviews : MMBR · 2014Review
- How Listeria monocytogenes organizes its surface for virulence.Frontiers in cellular and infection microbiology · 2014Review
- Listeria monocytogenes virulence factor secretion: don't leave the cell without a chaperone.Frontiers in cellular and infection microbiology · 2014Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
PrsA2 is a conserved posttranslocation chaperone and a peptidyl prolyl cis-trans isomerase (PPIase) that contributes to the virulence of the Gram-positive intracellular pathogen Listeria monocytogenes. One of the phenotypes associated with a prsA2 mutant is decreased activity of the broad-range phospholipase C (PC-PLC). PC-PLC is made as a proenzyme whose maturation is mediated by a metalloprotease (Mpl). The proforms of PC-PLC and Mpl accumulate at the membrane-cell wall interface until a decrease in pH triggers their maturation and rapid secretion into the host cell. In this study, we examined the mechanism by which PrsA2 regulates the activity of PC-PLC. We observed that in the absence of PrsA2, the proenzymes are secreted at physiological pH and do not mature upon a decrease in pH. The sensitivity of the prsA2 mutant to cell wall hydrolases was modified. However, no apparent changes in cell wall porosity were detected. Interestingly, synthesis of PC-PLC in the absence of its propeptide lead to the secretion of a fully active enzyme in the cytosol of host cells independent of PrsA2, indicating that neither the propeptide of PC-PLC nor PrsA2 is required for native folding of the catalytic domain, although both influence secretion of the enzyme. Taken together, these results suggest that PrsA2 regulates compartmentalization of Mpl and PC-PLC, possibly by influencing cell wall properties and interacting with the PC-PLC propeptide. Moreover, the ability of these proproteins to respond to a decrease in pH during intracellular growth depends on their localization at the membrane-cell wall interface.
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