Chapter 19 : PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen

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The facultative intracellular bacterium has been used for decades as a model infectious agent for the study of host innate and adaptive immunity. This chapter focuses on describing what is currently known about how mediates the transition from saprophyte to mammalian pathogen and explores the regulatory circuit governed by a transcriptional activator known as PrfA that allows the bacterium to flourish in both soil and cytosol. In healthy individuals, disease caused by is usually self-limiting and presents as a form of mild gastroenteritis. The primary route of infection is translocation across the intestinal epithelium following the consumption of contaminated food products. The correct compartmentalization of broad range phospholipase C (PC-PLC) activity is important for avoiding damage to host cell membranes and is a critical aspect of virulence. strains containing mutations are hyperinvasive, are quicker to mediate phagosome escape, and initiate bacterial actin-based motility more rapidly to promote cell-to-cell spread. Microarray analyses of wild-type and mutants grown in brain heart infusion broth suggest the possibility of at least 145 or more additional genes associated with PrfA regulation. PrfA activation appears to function as the switch that enables to transition from saprophyte to pathogen. In contrast to carbon sources encountered within the host, PrfA-dependent gene expression is dramatically repressed in the presence of cellobiose and other readily metabolized sugars that are likely to be more prevalent in environments located outside of host cells.

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19
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Figure 1

The L. monocytogenes transition from environmental bacterium to intracellular pathogen. L. monocytogenes survives under a number of diverse ecological conditions. It can be found growing within soil, decaying vegetation, water, silage, sewage, and food processing plants, but it also has the ability to adapt to life inside mammalian host cells. Central to the L. monocytogenes transition to life inside of host cells is the activity of a transcriptional regulator known as PrfA. Outside of host cells, PrfA exists in a low-activity state and directs low levels of virulence gene expression. Once inside a host, PrfA becomes highly activated (PrfA*) and dramatically increases the expression of a number of virulence gene products required for host cell invasion (internalins InlA and InlB), lysis of the phagosomal membrane (LLO, PI-PLC, and PC-PLC), intracellular growth (Hpt), cell-to-cell spread (actin assembly via ActA and relief of cell-cell cortical tension via InlC), and the dissolution of the double membrane resulting from cell-to-cell spread (LLO, PI-PLC, and PC-PLC). Adapted from Freitag et al. 2009.doi:10.1128/9781555818524.ch19f1

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19
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Figure 2

Transcriptional and posttranscriptional regulation of prfA. (A) Organization of the plcA-prfA region showing the location of all three promoter elements required for prfA expression. PprfAP1 and PprfAP2 are immediately upstream of prfA, while the third promoter, PplcA, is located upstream of plcA and directs both a monocistronic plcA transcript and a bicistronic plcAprfA transcript. Both PplcA and PprfAP1 contain characteristics of an sA-dependent promoter, while PprfAP2 contains characteristics of both sB- and sA-dependent promoters. The stem-loop structure indicates the plcA transcriptional terminator. The thermosensor is present within the 5¢ UTR of the prfAP1 transcript and inhibits prfAP1 translation at lower temperatures. Both PprfAP1 and PprfAP2 are negatively [(−)] influenced by high levels of PrfA, whereas PplcA is positively [(+)] influenced, resulting in the production of the increased quantities of PrfA required for intracellular growth and spread. (B) Model of SreA trans regulation of prfA expression. SAM binding to the SAM-responsive riboswitch SreA results in a conformational change to the transcript and a terminator structure is formed, which then leads to the production of a short transcript lacking the downstream genes. Complementary nucleotide regions shared between this sRNA transcript and the 5¢ UTR of the prfA mRNA result in a direct interaction between the two molecules that functions to reduce PrfA protein synthesis by blocking ribosome binding at 37°C. At lower temperatures (≤30°C), the thermosensor structure is formed at the 5¢ UTR of the prfA mRNA and prevents both SreA binding and prfA mRNA translation. doi:10.1128/9781555818524.ch19f2

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19
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Figure 3

Model of the PrfA putative cofactor binding pocket and location of PrfA* amino acid substitutions. (A) Electrostatic modeling of PrfA protein showing the distribution of solvent-accessible surface charges on the protein dimer. Positive charge is shown in blue and negative charge in red, with electrostatic potentials ranging from –4kT/e (red) to +4kT/e (blue). Arrows point to the lysine residues that contribute to the positive charge of the putative cofactor binding pocket within PrfA. The positive charge of the DNA binding region is also highlighted at the bottom of the PrfA monomer. Reprinted from PLoS One ( ) with permission of the publisher. (B) Ribbon modeling of the PrfA dimer using DeepView-Swiss PdbViewer v4.0 (http://spdbv.vital-it.ch/) highlighting the tunnel region (black arrow) suggested by Eiting et al., 2005, as the cofactor binding site. The monomers that make up the dimer are colored either light or dark gray, and the DNA-binding helix-turn-helices are shown in blue. The locations of amino acid substitutions conferring the PrfA* phenotype are colored as follows: Y63C in green, S71C in tan, E77K in magenta, A94T in dark blue, L140F in red, G145S in black, L148P in yellow, Y154C in light pink, G155S in light blue, and P219S in orange. Residues G145 and G155 are difficult to see in this orientation and have been further highlighted by arrows pointing to their location. doi:10.1128/9781555818524.ch19f3

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19
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Figure 4

The posttranslocation secretion chaperone PrsA2 is critical for L. monocytogenes viability under conditions of PrfA activation. PrsA2 is a secreted chaperone that contributes to the folding and stability of L. monocytogenes secreted virulence factors and penicillin binding proteins at the membrane-cell wall interface. Outside of host cells and under conditions of low PrfA activity, PrsA2 is synthesized in small amounts and assists in the folding of virulence factors secreted at low levels, such as LLO (top). When PrfA becomes activated following the entry of L. monocytogenes into the cytosol, protein secretion increases dramatically, with a concurrent increase in PrsA2 levels to help mediate secreted protein folding and stability (middle). Under conditions of PrfA activation in the absence of PrsA2, misfolded proteins accumulate at the membrane-cell wall interface and compromise bacterial viability within the cytosol (bottom). doi:10.1128/9781555818524.ch19f4

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19
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Figure 5

Model of prfA regulation during the L. monocytogenes transition from life in the outside environment to life inside the host. In the outside environment, low levels of PrfA protein are provided via transcripts directed from both the prfAP1 and prfAP2 promoters. The prfAP1 transcript contains a 5¢ RNA thermosensor that serves to inhibit prfAP1 translation at temperatures below 30°C. Low levels of PrfA protein are provided from the prfAP2 transcripts (upper row). Following bacterial ingestion by a mammalian host, an increase in temperature and the acidic environment of the stomach induces the activity of the stress-responsive RNA polymerase alternative sigma factor sB, leading to increased expression of prfA, inlA, and inlB via their sB-regulated promoters. A low-activity form of PrfA accumulates as a result of the increase in prfAP2 promoter activity. While the increase in temperature relieves the inhibition of prfAP1 translation imposed by the prfA thermosensor, prfAP1 translation may still be inhibited via the direct binding of the SreA riboswitch to the 5¢ UTR of prfAP1 transcripts (middle row). Once inside the host cell, PrfA-dependent production of LLO and PlcA mediates the efficient escape of L. monocytogenes from the phagosome into the cytosol, where unknown signals lead to the activation of PrfA and increased expression of prfA from the plcAP promoter. The plcA-prfA transcript results in the accumulation of increased levels of PrfA, which becomes activated via cofactor binding. High levels of activated PrfA increase the expression of a variety of gene products that contribute to L. monocytogenes intracellular replication and cell-to-cell spread (lower row). doi:10.1128/9781555818524.ch19f5

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19
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Figure 6

Model depicting the links between carbon transport and metabolism and PrfA-dependent virulence gene expression. The PEP-PTS is a multiprotein phosphorelay system that couples the transport of sugars across the bacterial membrane with their simultaneous phosphorylation. The PTS is comprised of three distinct proteins: EI, histidine protein (Hpr), and the permease EII. (Left) Outside of host cells, L. monocytogenes can be found in environments rich in the presence of PTSdependent sugars, such as the plant sugar cellobiose. Transport of PTS-dependent sugars into the bacterial cell initiates with the autophosphorylation of EI using the phosphoryl group from PEP. EI subsequently transfers a phosphoryl group to Hpr, which then transfers it to the A domain of the EII permease group. As the sugar is transported into the bacterial cell, the phosphoryl group of EIIA is rapidly transferred to the EIIB domain and then to the incoming sugar as it passes through the EIIC domain of the permease. EIIA is therefore in a nonphosphorylated state during active PTS sugar transport, and it is this nonphophorylated form of EIIA that has been proposed to sequester PrfA, thereby reducing or inhibiting its activity. (Right) Within the mammalian cell cytosol, alternative carbon sources such as hexose-phosphate sugars and C3 sugars appear to be the predominant sources of carbohydrates used by L. monocytogenes. Transport of these non-PTS-dependent sugars into the bacterial cell occurs either via facilitated diffusion or through alternative transporters such as the Hpt system. Sugar transport via these alternative pathways leaves the EIIA component of the PTS in its phosphorylated state. It has been proposed that phosphorylated EIIA cannot sequester PrfA, which is then free to bind a cofactor that may be produced either by the bacterial cell or by the host cell. Activated PrfA binds target promoters and induces the expression of multiple bacterial gene products that contribute to host infection. Adapted from Freitag et al., 2009. doi:10.1128/9781555818524.ch19f6

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19
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Table 1

Gene products directly or indirectly regulated by PrfA

Citation: Xayarath B, Freitag N. 2013. PrfA and the Switch from Environmental Bacterium to Intracellular Pathogen, p 363-385. In Vasil M, Darwin A (ed), Regulation of Bacterial Virulence. ASM Press, Washington, DC. doi: 10.1128/9781555818524.ch19

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