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Chapter 4 : Secretes Different Phospholipases A

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Secretes Different Phospholipases A, Page 1 of 2

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Abstract:

secretes several enzymes, including phospholipase A (PLA), via a -dependent type II secretion pathway. Phospholipases possess distinct substrate specificities with respect to both the phospho-head groups and the length and saturation of acyl chains esterified to the glycerol backbone. Although more frequently described for phospholipases C, PLAs are suspected to be virulence factors of bacteria. PLAs has been found for bacterial infections, phospholipases may be responsible for the bacterial escape from phagosomes and host cells after intracellular multiplication, the destruction of macrophages and epithelial cells, the generation of signal transducers like lyso-phosphatidylcholine and derivatives of both arachidonic and linoleic acid, the destruction of lung surfactant, and the induction of inflammation. The absence of dipalmitoylphosphatidylethanolamine (DPPE)-hydrolysis in the present study could be due to the high purity of DPPE (99%) or due to the high gel-to-liquid crystalline phase transition temperature of the palmitoyl derivate used in these experiments, whereas surfactant comprises a mixture of several phospholipids with distinct esterified fatty acids. The hydrolysis of both monopalmitoyl lysophosphatidylcholine (MPLPC) and 1-monopalmitoylglycerol (1-MPG) by lysophospholipase A (LPLA) corresponds to the substrate specificities of the enzyme family to which LPLA may belong, comprising Upases, phospholipases A, esterases, and acyltransferases. Since PLA and LPLA of are potent in destruction of a variety of phospholipids and the composition of membranes of different cell membranes varies considerably, they might affect many cell types.

Citation: Flieger A, Cianciotto N, Gong S, Faigle M, Northoff H, Neumeister B, Stevanovic S. 2002. Secretes Different Phospholipases A, p 22-26. In Marre R, Abu Kwaik Y, Bartlett C, Cianciotto N, Fields B, Frosch M, Hacker J, Lück P (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555817985.ch4

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Fatty Acids
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Acute Respiratory Distress Syndrome
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Figures

Image of FIGURE 1
FIGURE 1

Release of fatty acids by 10-fold concentrated CCS of from different lipids. DPPG, DPPC, DPPE, phosphatidylinositol (PI), dipalmitoylphosphatidylserine (DPPS), sphingomyeline (Sph), MPLPC, LPG, and 1-MPG were incubated with CCS for 5 h. Data are means ± standard deviation of four experiments and are shown as the difference between release of fatty acids by CCS and by negative control (20 mM Tris-HCl, pH 7.2).

Citation: Flieger A, Cianciotto N, Gong S, Faigle M, Northoff H, Neumeister B, Stevanovic S. 2002. Secretes Different Phospholipases A, p 22-26. In Marre R, Abu Kwaik Y, Bartlett C, Cianciotto N, Fields B, Frosch M, Hacker J, Lück P (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555817985.ch4
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Image of FIGURE 2
FIGURE 2

Separation of 's lipolytic activities by AEC. 10-fold concentrated bacterial supernatant from a 5000-ml culture supernatant was subjected to AEC. Fractions (10 ml) eluted from 0 to 1 Μ sodium chloride were investigated for protein content and FFA release during a 1-h incubation with DPPG, DPPC, MPLPC, and 1-MPG. Reducing SDS-PAGE was performed on fractions 15 to 20, and the separated proteins were visualized by silver staining. St, molecular weight standard; numbers to the left indicate molecular mass (in kilodaltons). The 28-kDa protein band is designated by the arrow. The experiment shown is representative of 10 additional trials. Reprinted from reference 8 with permission.

Citation: Flieger A, Cianciotto N, Gong S, Faigle M, Northoff H, Neumeister B, Stevanovic S. 2002. Secretes Different Phospholipases A, p 22-26. In Marre R, Abu Kwaik Y, Bartlett C, Cianciotto N, Fields B, Frosch M, Hacker J, Lück P (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555817985.ch4
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Image of FIGURE 3
FIGURE 3

Release of FFA from DPPG, DPPC, MPLPC, and 1-MPG by culture supernatants of L. pneumophila in comparison to a -deficient mutant. Legionellae were grown in buffered yeast extract (BYE) broth. Lipolytic activities were determined by detection of FFA release after incubation of culture supernatant with DPPG, DPPC, MPLPC, and 1-MPG, respectively, for 15 h. Data are means ± standard deviation of four experiments and are shown as the difference between fatty acids released by bacterial supernatant and by negative control (BYE broth).

Citation: Flieger A, Cianciotto N, Gong S, Faigle M, Northoff H, Neumeister B, Stevanovic S. 2002. Secretes Different Phospholipases A, p 22-26. In Marre R, Abu Kwaik Y, Bartlett C, Cianciotto N, Fields B, Frosch M, Hacker J, Lück P (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555817985.ch4
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References

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1. Aragon, V.,, S. Kurtz,, A. Flieger,, B. Neumeister,, and N. P. Cianciotto. 2000. Secreted enzymatic activities of wild-type and pilD-deficient Legionella pneumophila. Infect. Immun. 68:18551863.
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11. Liles, M. R.,, P. H. Edelstein,, and N. P. Cianciotto. 1999. The prepilin peptidase is required for protein secretion by and the virulence of the intracellular pathogen Legionella pneumophila. Mol. Microbiol. 31:959970.
12. Neumeister, B.,, S. Schoniger,, M. Faigle,, M. Eichner,, and K. Dietz. 1997. Multiplication of different Legionella species in Mono Mac 6 cells and in Acanthamoeba castellanii. Appl. Environ. Miaobiol. 63:12191224.
13. Rossier, O.,, and N. P. Cianciotto. 2001. sType II protein secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila. Infect. Immun. 69:20922098.
14. Simons, J. W.,, F. Gotz,, M. R. Egmond, and H. M. Verheij. 1998. Biochemical properties of staphylococcal (phospho)lipases. Chem. Phys. Lipids 93:2737.

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