ArticleMicrobiology (Reading, England)2008
Functional impact of mutational activation on the Listeria monocytogenes central virulence regulator PrfA.
Article in Microbiology (Reading, England), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 49 citations in OpenAlex.
- Transcriptional responses of Listeria monocytogenes to low-temperature stress reveal distinct adaptive mechanisms in the absence of BKD and PrfA activation.Microbial pathogenesis · 2025Article
- Listeria monocytogenes: from a saprophytic to a cytosolic virulent pathogen.World journal of microbiology & biotechnology · 2025Review
- Listeria monocytogenes requires phosphotransferase systems to facilitate intracellular growth and virulence.PLoS pathogens · 2025Article
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- Article
- Role of FruR transcriptional regulator in virulence of Listeria monocytogenes and identification of its regulon.PloS one · 2022Article
- Rhizobacteria Impact Colonization of Listeria monocytogenes on Arabidopsis thaliana Roots.Applied and environmental microbiology · 2021Article
- Identification of Listeria monocytogenes Genes Contributing to Oxidative Stress Resistance under Conditions Relevant to Host Infection.Infection and immunity · 2021Article
- Free Fatty Acids Interfere with the DNA Binding Activity of the Virulence Regulator PrfA of Listeria monocytogenes.Journal of bacteriology · 2020Article
- Regulation ofMicrobiology spectrum · 2019Review
- Relative Roles of Listeriolysin O, InlA, and InlB in Listeria monocytogenes Uptake by Host Cells.Infection and immunity · 2018Article
- Activation of themBio · 2017Article
- Secretion Chaperones PrsA2 and HtrA Are Required for Listeria monocytogenes Replication following Intracellular Induction of Virulence Factor Secretion.Infection and immunity · 2016Article
- An In Vivo Selection Identifies Listeria monocytogenes Genes Required to Sense the Intracellular Environment and Activate Virulence Factor Expression.PLoS pathogens · 2016Article
- Perforin-2 Protects Host Cells and Mice by Restricting the Vacuole to Cytosol Transitioning of a Bacterial Pathogen.Infection and immunity · 2016Article
- Host actin polymerization tunes the cell division cycle of an intracellular pathogen.Cell reports · 2015Article
- Identification of a peptide-pheromone that enhances Listeria monocytogenes escape from host cell vacuoles.PLoS pathogens · 2015Article
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- PrfA-like transcription factor gene lmo0753 contributes to L-rhamnose utilization in Listeria monocytogenes strains associated with human food-borne infections.Applied and environmental microbiology · 2013Article
- Processing of recombinant Listeria monocytogenes proteins for MHC class I presentation follows a dedicated, high-efficiency pathway.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The transcriptional activator PrfA is required for the expression of virulence factors necessary for Listeria monocytogenes pathogenesis. PrfA is believed to become activated following L. monocytogenes entry into the cytosol of infected host cells, resulting in the induction of target genes whose products are required for bacterial intracellular growth and cell-to-cell spread. Several mutations have been identified that appear to lock PrfA into its highly activated cytosolic form (known as prfA* mutations). In this study PrfA and five PrfA* mutant proteins exhibiting differing degrees of activity were purified and analysed to define the influences of the mutations on distinct aspects of PrfA activity. Based on limited proteolytic digestion, conformational changes were detected for the PrfA* mutant proteins in comparison to wild-type PrfA. For all but one mutant (PrfA Y63C), the DNA binding affinity as measured by electophoretic mobility shift assay appeared to directly correlate with levels of PrfA mutational activation, such that the high-activity mutants exhibited the largest increases in DNA binding affinity and moderately activated mutants exhibited more moderate increases. Surprisingly, the ability of PrfA and PrfA* mutants to form dimers in solution appeared to inversely correlate with levels of PrfA-dependent gene expression. Based on comparisons of protein activity and structural similarities with PrfA family members Crp and CooA, the prfA* mutations modify distinct aspects of PrfA activity that include DNA binding and protein-protein interactions.
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Registered trials
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