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Chapter 5 : In Vitro Secretion Kinetics of Compared with Those of Non- Species

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In Vitro Secretion Kinetics of Compared with Those of Non- Species, Page 1 of 2

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Abstract:

This chapter characterizes the secretion kinetics of putative virulence factors of in comparison with those of non- species during the phase of growth, when nutritional factors may become limited. To investigate the secretion pattern of different species, culture supernatants were evaluated for acid phosphatase, protease, phospholipase A (PLA), and lysophospholipase A (LPLA) activities. The experiments revealed that the examined enzyme activities seem to be secreted throughout the whole genus, except and lack the majority of the activities tested. Differences in PLA secretion of different isolates within one species () have been described. , , and exhibited the highest PLA activity, and both and one of the tested strains exhibited the most prominent LPLA activity. To estimate the amount of lysophosphatidylcholine (LPC) generated from culture supernatants of different species, the authors incubated culture supernatants with dipalmitoylphosphatidylchohne (DPPC) and analyzed the lipids by thin-layer chromatography. Culture supernatants from the exponential growth phase of both and generated considerable amounts of LPC. LPC was also produced by but not before bacteria entered the stationary phase.

Citation: Flieger A, Gong S, Faigle M, Northoff H, Neumeister B. 2002. In Vitro Secretion Kinetics of Compared with Those of Non- Species, p 27-30. 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.ch5

Key Concept Ranking

Legionella pneumophila
0.71386224
Phospholipase A
0.625
0.71386224
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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.
2. Aronson, J. F.,, and L. W. Johns. 1977. Injury of lung alveolar cells by lysolecithin. Exp. Mol. Pathol. 27:3542.
3. Dennis, E. A. 1997. The growing phospholipase A2 superfamily of signal transduction enzymes. Trends Biochem. Sci. 22:12.
4. 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.
5. Flieger, A.,, S. Gong,, M. Faigle,, H. A. Mayer,, U. Kehrer,, J. MuPotter,, P. Bartmann,, and B. Neumeister. 2000. Phospholipase A secreted by Legionella pneumophila destroys alveolar surfactant phospholipids. FEMS Microbiol. Lett. 188:129133.
6. 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.
7. Holm, B. A.,, L. Keicher,, M. Y. Liu,, J. Sokolowski,, and G. Enhorning. 1991. Inhibition of pulmonary surfactant function by phospholipases. J. Appl. Physiol. 71:317321.
8. Kume, N.,, M. I. Cybulsky,, and M. A. Gimbrone, Jr. 1992. Lysophosphatidylcholine, a component of atherogenic lipoproteins, induces mononuclear leukocyte adhesion molecules in cultured human and rabbit arterial endothelial cells. J. Clin. Invest. 90:11381144.
9. 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.
10. Lindahl, M.,, A. R. Hede,, and C. Tagesson. 1986. Lysophosphatidylcholine increases airway and capillary permeability in the isolated perfused rat lung. Exp. Lung Res. 11:112.
11. 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. Microbiol. 63:12191224.
12. Niewoehner, D. E.,, K. Rice,, A. A. Sinha,, and D. Wangensteen. 1987. Injurious effects of lysophosphatidylcholine on barrier properties of alveolar epithelium. J. Appl. Physiol. 63:19791986.
13. Prokazova, N. V.,, N. D. Zvezdina,, and A. A. Korotaeva. 1998. Effect of lysophosphatidylcholine on transmembrane signal transduction. Biochem. Mosc. 63:3137.
14. Weltzien, H. U. 1979. Cytolytic and membrane-perturbing properties of lysophosphatidylcholine. Biochim. Biophys. Acta 559:259287.

Tables

Generic image for table
TABLE 1

strains used and maximal enzyme activities of their culture supernatants

Citation: Flieger A, Gong S, Faigle M, Northoff H, Neumeister B. 2002. In Vitro Secretion Kinetics of Compared with Those of Non- Species, p 27-30. 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.ch5
Generic image for table
TABLE 2

Generation of LPC after incubation of DPPC with culture supernatants of different species and strains from different times of growth in BYE broth

Citation: Flieger A, Gong S, Faigle M, Northoff H, Neumeister B. 2002. In Vitro Secretion Kinetics of Compared with Those of Non- Species, p 27-30. 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.ch5

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