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Chapter 57 : Phospholipases A of : Virulence Factors by Diversity?

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Phospholipases A of : Virulence Factors by Diversity?, Page 1 of 2

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Abstract:

possesses several virulence mediating factors; for example, it has two protein export systems: the type II (Lsp) and the type IVB (Dot/Icm) secretion systems. Both systems transport effector molecules, including lipolytic proteins such as phospholipases. possesses two major phospholipase activities, phospholipase A (PLA) and lysophospholipase A (LPLA), both capable of hydrolyzing phospholipids and generating the reaction products: free fatty acids (PLA and LPLA), cytotoxic lysophospholipids (via the action of PLA), and water-soluble phosphodiesters, like glycerophosphorylcholine (via the subsequent action of LPLA on lysophospholipids). Patatins are a group of plant storage glycoproteins that show lipid acyl hydrolase activity. One of the corresponding proteins, PatA, was found to be an LPLA when expressed in . The to genes of have been determined to be expressed during bacterial growth in laboratory media. Furthermore, by the construction of knockout mutants, it was shown that contributes to secreted bacterial PLA and LPLA activities and is essential for intracellular replication of , during both amoeba and macrophage infection, which implies an important role for lipolytic enzymes with respect to the pathogenic behavior of the bacterium. The high number of lipolytic enzymes present in implies that lipids may be an important source of nutrients for the bacterium, and/or lipid hydrolysis is an essential step in bacterial establishment, especially within the host cell.

Citation: Flieger A. 2006. Phospholipases A of : Virulence Factors by Diversity?, p 228-231. In Cianciotto N, Kwaik Y, Edelstein P, Fields B, Geary D, Harrison T, Joseph C, Ratcliff R, Stout J, Swanson M (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555815660.ch57

Key Concept Ranking

Type IVB Secretion System
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Figures

Image of FIGURE 1
FIGURE 1

Overview of the secreted and cell-associated PLA, LPLA, and acyl-transferase activities of The protein with only LPLA activity is PlaA. PlaB, PlaD, and PatA/VipD possess PLA and LPLA activities. In addition to PLA and LPLA activity, PlaC confers an acyltransferase activity and is directly or indirectly activated by the zinc-metalloprotease ProA. PatB to PatK represent so far uncharacterized putative lipolytic proteins. Furthermore, the dependency on specific secretion systems (Lsp = type II secretion, Dot/Icm = type IVB secretion) is shown or unknown (designated by ?). Proteins whose activity or expression depends on host cell contact are shown in proximity to the host cell.

Citation: Flieger A. 2006. Phospholipases A of : Virulence Factors by Diversity?, p 228-231. In Cianciotto N, Kwaik Y, Edelstein P, Fields B, Geary D, Harrison T, Joseph C, Ratcliff R, Stout J, Swanson M (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555815660.ch57
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References

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1. Banerji, S.,, M. Bewersdorff,, B. Hermes,, N. P. Cianciotto, and, A. Flieger. 2005. Characterization of the major secreted zinc metalloprotease-dependent glycerophospholipid:cholesterol acyl-transferase, PlaC, of Legionella pneumophila. Infect. Immun. 73:28992909.
2. Banerji, S. and, A. Flieger. 2004. Patatin-like proteins: a new family of lipolytic enzymes present in bacteria? Microbiology 150:522525.
3. Flieger, A.,, S. Gong,, M. Faigle,, M. Deeg,, P. Bartmann, and, B. Neumeister. 2000. Novel phospholipase A activity secreted by Legionella species. J. Bacteriol. 182:13211327.
4. Flieger, A.,, S. Gong,, M. Faigle,, S. Stevanovic,, N. P. Cianciotto, and, B. Neumeister. 2001. Novel lysophospholipase A secreted by Legionella pneumophila. J. Bacteriol. 183:21212124.
5. Flieger, A.,, B. Neumeister, and, N. P. Cianciotto. 2002. Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine. Infect. Immun. 70:60946106.
6. Flieger, A.,, K. Rydzewski,, S. Banerji,, M. Broich, and, K. Heuner. 2004. Cloning and characterization of the gene encoding the major cell-associated phospholipase A of Legionella pneumophila, plaB, exhibiting hemolytic activity. Infect. Immun. 72:26482658.
7. Rossier, O., and, N. P. Cianciotto. 2001. Type II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila. Infect. Immun. 69:20922098.
8. Sato, H.,, D. W. Frank,, C. J. Hillard,, J. B. Feix,, R. R. Pankhaniya,, K. Moriyama,, V. Finck-Barbancon,, A. Buchaklian,, M. Lei,, R. M. Long,, J. Wiener-Kronish, and, T. Sawa. 2003. The mechanism of action of the Pseudomonas aeruginosa-encoded type III cytotoxin, ExoU. EMBO J. 22:29592969.
9. Shohdy, N.,, J. A. Efe,, S. D. Emr, and, H. A. Shuman. 2005. Pathogen effector protein screening in yeast identifies Legionella factors that interfere with membrane trafficking. Proc. Natl. Acad. Sci. USA 102:48664871.
10. Upton, C., and, J. T. Buckley. 1995. A new family of lipolytic enzymes? Trends Biochem. Sci. 20:178179.

Tables

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TABLE 1

Overview of the PLA activities of their biochemical activities, localization, secretion type, and enzyme classification type

Citation: Flieger A. 2006. Phospholipases A of : Virulence Factors by Diversity?, p 228-231. In Cianciotto N, Kwaik Y, Edelstein P, Fields B, Geary D, Harrison T, Joseph C, Ratcliff R, Stout J, Swanson M (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555815660.ch57

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