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Chapter 54 : Identification of Putative Substrates of the Tat Secretion Pathway via Two-Dimensional Protein Gel Electrophoresis

Authors: E. De Buck1, L. Maes2, J. Robben3, J.-P. Noben4, J. Anné5, E. Lammertyn6
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Affiliations: 1: Laboratory of Bacteriology, Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium; 2: Laboratory of Bacteriology, Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium; 3: Biomedical Research Institute, Hasselt University, Agoralaan, Building A, B-3590 Diepenbeek, Belgium; 4: Biomedical Research Institute, Hasselt University, Agoralaan, Building A, B-3590 Diepenbeek, Belgium; 5: Laboratory of Bacteriology, Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium; 6: Laboratory of Bacteriology, Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Leuven, Belgium
Content Type: Monograph
Publication Year: 2006

Category: Bacterial Pathogenesis

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Identification of Putative Substrates of the Tat Secretion Pathway via Two-Dimensional Protein Gel Electrophoresis, Page 1 of 2

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Abstract:

Different secretion pathways have been shown to play a role in the virulence of . Recently the authors showed the presence of the twin-arginine translocation (Tat) pathway in Philadelphia-1 and its importance in intracellular replication and biofilm formation. The Tat pathway translocates folded proteins across the cytoplasmic membrane. In order to study the importance of the Tat pathway in the virulence of , the identification of Tat substrates and their possible involvement in virulence was initiated. Since some Tat substrates might be transported across the outer membrane following Tat-dependent transport across the cytoplasmic membrane, the authors looked for differential spots in culture media of the wild-type strain and two Tat secretion mutants ( and mutant) by two-dimensional protein gel electrophoresis analysis. Three proteins were found to be absent from the culture medium of the Tat secretion mutants: LvrE, Lpg1962 (a peptidyl-prolyl cis-trans isomerase), and Lpg2320 (a hypothetical protein). The gene is situated in between the ( homologues) genes on the Philadelphia-1 genome that encode the Lvh type IV secretion system. Based on two-dimensional analysis, three proteins were found to be absent in the culture media of the and mutant. For one of these proteins, LvrE, Tat dependence was confirmed using specific antibodies.

Citation: Buck E, L. Maes, J. Robben, J.-P. Noben, J. Anné, E. Lammertyn. 2006. Identification of Putative Substrates of the Tat Secretion Pathway via Two-Dimensional Protein Gel Electrophoresis, p 217-220. 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.ch54
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Identification of Putative Substrates of the Legionella pneumophila Tat Secretion Pathway via Two-Dimensional Protein Gel Electrophoresis
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Citation: Buck E, L. Maes, J. Robben, J.-P. Noben, J. Anné, E. Lammertyn. 2006. Identification of Putative Substrates of the Tat Secretion Pathway via Two-Dimensional Protein Gel Electrophoresis, p 217-220. 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.ch54
/content/10.1128/9781555815660.ch54.ch54fig01
FIGURE 1
Two-dimensional gel electrophoresis (12.5% acrylamide; pi 4 to 7) on the supernatant of Philadelphia-1 wild type (A) and mutant (B). 1, LvrE; 2, 3, LvrE fragments; 4, Lpg1962; 5, Lpg2320; 6, IcmX.
10.1128/9781555815660/f0218-01_thmb.gif
10.1128/9781555815660/f0218-01.gif
Image of FIGURE 1
FIGURE 1

Two-dimensional gel electrophoresis (12.5% acrylamide; pi 4 to 7) on the supernatant of Philadelphia-1 wild type (A) and mutant (B). 1, LvrE; 2, 3, LvrE fragments; 4, Lpg1962; 5, Lpg2320; 6, IcmX.

Citation: Buck E, L. Maes, J. Robben, J.-P. Noben, J. Anné, E. Lammertyn. 2006. Identification of Putative Substrates of the Tat Secretion Pathway via Two-Dimensional Protein Gel Electrophoresis, p 217-220. 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.ch54
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/content/10.1128/9781555815660.ch54.ch54fig02
FIGURE 2
Replication of wild type (white), mutant (grey) and complemented mutant (striped) in (A) and differentiated U937 cells (B).
10.1128/9781555815660/f0219-01_thmb.gif
10.1128/9781555815660/f0219-01.gif
Image of FIGURE 2
FIGURE 2

Replication of wild type (white), mutant (grey) and complemented mutant (striped) in (A) and differentiated U937 cells (B).

Citation: Buck E, L. Maes, J. Robben, J.-P. Noben, J. Anné, E. Lammertyn. 2006. Identification of Putative Substrates of the Tat Secretion Pathway via Two-Dimensional Protein Gel Electrophoresis, p 217-220. 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.ch54
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References

/content/book/10.1128/9781555815660.ch54
1. Berks, B. C.,, T. Palmer, and, F. Sargent. 2003. The Tat protein translocation pathway and its role in microbial physiology. Adv. Microb. Physiol. 47: 187— 254.
2. De Buck, E.,, I. Lebeau,, L. Maes,, N. Geukens,, E. Meyen,, L. Van Mellaert,, J. Anné, and, E. Lammertyn. 2004. A putative twin-arginine translocation pathway in Legionella pneumophila. Biochem. Biophys. Res. Commun. 317: 654— 661.
3. De Buck, E.,, L. Maes,, E. Meyen,, L. Van Mel-laert,, N. Geukens,, J. Anné, and, E. Lammer-tyn. 2005. Legionella pneumophila Philadelphia-1 tatB and tatC affect intracellular replication and biofilm formation. Biochem. Biophys. Res. Commun. 331: 1413— 1420.
4. Lammertyn, E., and, J. Anné. 2004. Protein secretion in Legionella pneumophila and its relation to virulence. FEMS Microbiol. Lett. 238: 273— 279.
5. Matthews, M., and, C. R. Roy. 2000. Identification and subcellular localization of the Legionella pneumophila IcmX protein: a factor essential for establishment of a replicative organelle in eukary-otic host cells. Infect. Immun. 68: 3971— 3982.
6. Segal, G.,, J. J. Russo, and, H. A. Shuman. 1999. Relationships between a new type IV secretion system and the icm/ dot virulence system of Legionella pneumophila. Mol. Microbiol. 34: 799— 809.
7. Sexton, J. A., and, J. P. Vogel. 2004. Regulation of hypercompetence in Legionella pneumophila. J. Bacteriol. 186: 3814— 3825.

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