Pleiotropic control of <i>Listeria monocytogenes</i> virulence factors by a gene that is autoregulated

Mengaud, J; Dramsi, Shaynoor; Gouin, Edith; Vázquez‐Boland, José A.; Milon, Geneviève; Cossart, Pascale

doi:10.1111/j.1365-2958.1991.tb02158.x

Cited by 256 publications

(281 citation statements)

References 31 publications

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“…The factors required for intracellular survival are encoded by the major virulence locus of L. monocytogenes. They include the secreted listeriolysin O (LLO) and two phospholipases involved in the disruption of phagosomal membranes and bacterial escape to the cytoplasm Mengaud et al 1987;Váz-quez-Boland et al 1992), the surface protein ActA that mediates the polymerization of cytoplasmic actin (Domann et al 1992;Kocks et al 1992) and favors cell-to-cell spread (Tilney and Portnoy 1989) as well as PrfA, the transcriptional activatorof bacterial virulence genes (Leimeister-Wächter et al 1990;Mengaud et al 1991). Comparative genomic approaches on the pathogenic L. monocytogenes and the nonpathogenic Listeria innocua has led in recent years to the identification of many additional bacterial factors required for infection (Camejo et al 2011;Cossart 2011).…”

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confidence: 99%

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

Pizarro‐Cerdá

Kühbacher

Cossart

2012

Cold Spring Harbor Perspectives in Medicine

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Listeria monocytogenes is a bacterial pathogen that promotes its internalization into host epithelial cells. Interaction between the bacterial surface molecules InlA and InlB and their cellular receptors E-cadherin and Met, respectively, triggers the recruitment of endocytic effectors, the subversion of the phosphoinositide metabolism, and the remodeling of the actin cytoskeleton that lead to bacterial engulfment. Additional bacterial surface and secreted virulence factors also contribute to entry, albeit to a lesser extent. Here we review the increasing number of signaling effectors that are reported as being subverted by L. monocytogenes during invasion of cultured cell lines. We also update the current knowledge of the early steps of in vivo cellular infection, which, as shown recently, challenges previous concepts generated from in vitro data.

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confidence: 99%

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

Pizarro‐Cerdá

Kühbacher

Cossart

2012

Cold Spring Harbor Perspectives in Medicine

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203

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“…In vitro transcription starting at P plcA and P aroA Transcription starting at the promoter of plcA (P plcA ) has been shown previously to be dependent on PrfA (Leimeister-Wächter et al ., 1991;Mengaud et al ., 1991;Lalic-Mülthaler et al ., 2001). The PrfA binding site of P plcA possesses a perfect dyad symmetry (Kreft and Vázquez-Boland, 2001; see also Fig.…”

Section: Resultsmentioning

confidence: 99%

“…a PrfA-box and a -10 box recognized by SigA-loaded RNA polymerase in an appropriate distance (Luo et al, 2004), do not function as PrfA-dependent promoters. For this goal we compared the plcA promoter, which is functional as PrfA-dependent promoter as demonstrated in vivo and in vitro (Mengaud et al, 1991;Sheehan et al, 1995;Böckmann et al, 2000;Lalic-Mülthaler et al, 2001), with an upstream regulatory sequence of the aroA gene (termed ParoA2) which contains a similar PrfA-box and a -10 site (in the same distance) as PplcA but does not function as PrfA-dependent promoter.…”

Section: Figmentioning

confidence: 99%

“…The regulatory protein PrfA is the major transcription activator of most of the known virulence genes of the two pathogenic Listeria species, L. monocytogenes and L. ivanovii (Leimeister-Wächter et al ., 1990;Mengaud et al ., 1991;Chakraborty et al ., 1992;Lampidis et al ., 1994;Vázquez-Boland et al ., 2001). This protein belongs to the Crp/Fnr family of transcription activators which control many genes and operons in Gram-negative and Grampositive bacteria (Busby and Ebright, 1994;1999;Lampidis et al ., 1994;Kreft and Vázquez-Boland, 2001; Körner et al ., 2003;Reid et al ., 2004).…”

Section: Introductionmentioning

confidence: 99%

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Supportive and inhibitory elements of a putative PrfA‐dependent promoter inListeria monocytogenes

Luo

Herler

Müller-Altrock

et al. 2005

Molecular Microbiology

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SummaryElements essential for PrfA-dependent transcription were analysed on two promoters of Listeria monocytogenes , the PrfA-dependent promoter of the phospholipase gene plcA (P plcA ) and a putative promoter of the aroA gene (P aroA2 ) which contains a similar PrfA-binding site and a similar ----10 box as P plcA but does not function as PrfA-dependent promoter. We constructed a series of hybrid plcA-aroA promoters by exchanging corresponding sequence elements of these two 'promoters'. The results showed that the two critical elements of PrfA-dependent promoters, the PrfA-box and the ----10 box, can be functionally exchanged as long as the distance in between is maintained to 22 or 23 bp. However, the interspace sequence and the sequence downstream of the ----10 box of P aroA2 were strongly inhibitory for PrfAdependent transcription. A detailed analysis of these two sequences revealed that the RNA polymerase binding site being part of the actual in vivo and in vitro used aroA promoter (P aroA1 ) and a sequence immediately downstream of the putative ----10 site, possibly blocking the formation of the open complex, were responsible for the inhibition of PrfA-dependent transcription from P aroA2 . Taking into consideration the lessons learned from this study we were able to construct a functional PrfA-dependent aroA promoter.

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“…The gene for PI-PLC, plcA, is in a cluster of virulence-associated chromosomal genes which are controlled by PrfA, a positive regulatory protein (4,5,13,20). Only pathogenic Listeria species secrete PI-PLC (12,19,21).…”

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Listeria monocytogenes phosphatidylinositol (PI)-specific phospholipase C has low activity on glycosyl-PI-anchored proteins

1993

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The ability of the phosphatidylinositol-specific phospholipase C (PI-PLC) from Listeria monocytogenes to hydrolyze glycosyl phosphatidylinositol (GPI)-anchored membrane proteins was compared with the ability of the PI-PLC from Bacillus thuringiensis to hydrolyze such proteins. The L. monocytogenes enzyme produced no detectable release of acetylcholinesterase from bovine, sheep, and human erythrocytes. The cleavage of the GPI anchors of alkaline phosphatase from rat and rabbit kidney slices was less than 10% of the cleavage seen with the PI-PLC from B. thuringiensis. Activity for release of Fcy receptor IIIB (CD16) on human granulocytes was also low. Variations in pH and salt concentration had little effect on the release of GPI-anchored proteins. Our data show that L. monocytogenes PI-PLC has low activity on GPI-anchored proteins.Phosphatidylinositol-specific phospholipase C (PI-PLC) is secreted by Several species of gram-positive bacteria, including the human pathogens Staphylococcus aureus (16), Clostridium novyi (26), and Bacillus anthracis (14). However, a role for this enzyme in the pathogenesis of the diseases caused by these organisms has not been defined. Recently, PI-PLC was identified as one of several proteins secreted by Listeria monocytogenes, a facultatively intracellular human and animal pathogen (3,12,19). The protein has been overexpressed in L. monocytogenes, purified to homogeneity, and characterized with respect to substrate specificity and in vitro requirements for enzyme activity (7). Like other prokaryotic PI-PLCs, the L. monocytogenes enzyme was found to be specific for phosphatidylinositol (PI) and to have no detectable activity on phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate, which are involved in signal transduction in mammalian cells (1).Bacterial PI-PLCs were originally discovered as a result of their ability to cleave glycosyl-phosphatidylinositol (GPI)-anchored membrane proteins at the PI terminus (14, 15), and all bacterial PI-PLCs appear to possess this activity. When the purified enzyme from L. monocytogenes was tested on the membrane form of the variant surface glycoprotein of Trypanosoma brucei, it was able to cleave the GPI anchor; however, its activity was approximately 10% of the activity of the PI-PLC from Bacillus thuringiensis when equivalent PI hydrolysis units were compared (7). Since GPI-anchored proteins are potential targets for this facultatively intracellular pathogen during its entry into host cells by phagocytosis (3, 19) and subsequent escape from phagocytic vacuoles (4), we further explored the ability of L. monocytogenes PI-PLC (PT-PLCL.m.) to release these proteins from cell membranes. Our data show that this enzyme has little or no activity for * Corresponding author. GPI-anchored proteins obtained from a variety of human and animal tissues.Release of acetylcholinesterase from erythrocytes. Erythrocytes (bovine and sheep cells obtained from Rockland, Inc., Gilbertsville, Pa.; human erythrocytes obtained from peripheral blood of...

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Pleiotropic control of Listeria monocytogenes virulence factors by a gene that is autoregulated

Cited by 256 publications

References 31 publications

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

Entry of Listeria monocytogenes in Mammalian Epithelial Cells: An Updated View

Supportive and inhibitory elements of a putative PrfA‐dependent promoter inListeria monocytogenes

Listeria monocytogenes phosphatidylinositol (PI)-specific phospholipase C has low activity on glycosyl-PI-anchored proteins

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