ArticleMolecular microbiology2016
A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence.
Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 26 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
- Crystal structure and biophysical characterisation of the enterococcal foldase PpiC, a cross-opsonic antigen against gram-positive nosocomial pathogens.The FEBS journal · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Characterization of theInfection and immunity · 2025Article
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- Insights into mechanisms and significance of domain swapping from emerging examples in the Mog1p/PsbP-like fold.Biochemical and biophysical research communications · 2025Review
- Structural analysis of extracellular ATP-independent chaperones of streptococcal species and protein substrate interactions.mSphere · 2025Article
- The chaperone PrsA2 regulates the secretion, stability, and folding of listeriolysin O duringmBio · 2024Article
- Revisiting old friends: updates on the role of two-component signaling systems inInfection and immunity · 2024Review
- Staphylococcus aureus foldase PrsA contributes to the folding and secretion of protein A.BMC microbiology · 2024Article
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- Review
- Listeria monocytogenes two component system PieRS regulates secretion chaperones PrsA1 and PrsA2 and enhances bacterial translocation across the intestine.Molecular microbiology · 2022Article
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- Deletion of a Peptidylprolyl Isomerase Gene Results in the Inability ofApplied and environmental microbiology · 2020Article
- An mRNA-mRNA Interaction Couples Expression of a Virulence Factor and Its Chaperone in Listeria monocytogenes.Cell reports · 2020Article
- Identification and optimization of PrsA in Bacillus subtilis for improved yield of amylase.Microbial cell factories · 2019Article
- The conserved mosaic prophage protein paratox inhibits the natural competence regulator ComR in Streptococcus.Scientific reports · 2018Article
- PrsA2 (CD630_35000) ofFrontiers in microbiology · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Listeria monocytogenes is a Gram-positive environmental bacterium that lives within soil but transitions into a pathogen upon contact with a mammalian host. The transition of L. monocytogenes from soil dweller to cytosolic pathogen is dependent upon secreted virulence factors that mediate cell invasion and intracellular growth. PrsA1 and PrsA2 are secreted bacterial lipoprotein chaperones that contribute to the folding of proteins translocated across the bacterial membrane; PrsA2 is required for L. monocytogenes virulence, whereas the function of PrsA1 remains to be determined. We have solved an X-ray crystal structure of PrsA1 and have used this model to guide comparison structure-based mutagenesis studies with PrsA2. Targeted mutagenesis of PrsA2 demonstrates that oligomerization of PrsA2 as well as molecular features of the foldase domain are required for protein secretion and virulence, whereas a functional role was uncovered for PrsA1 in bacterial resistance to alcohol. Interestingly, PrsA2 membrane localization is not required for all PrsA2-dependent activities, suggesting that the lipoprotein retains function when released from the bacterial cell. PrsA chaperones are thus multifaceted proteins with distinct domains adapted to accommodate the functional needs of a diverse array of secreted substrates.
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