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Chapter 55 : Identification of Target Proteins of the Lss Secretion System of Corby

Authors: Christiane Albert1, Sebastian Jacobi2, Emmy De Buck3, Elke Lammertyn4, Klaus Heuner5
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Affiliations: 1: Institut für Molekulare Infektionsbiologie, Julius-Maximilians Universität Würzburg, Röntgenring 11, D-97070 Würzburg, Germany; 2: Institut für Molekulare Infektionsbiologie, Julius-Maximilians Universität Würzburg, Röntgenring 11, D-97070 Würzburg, Germany; 3: Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Louvain, Belgium; 4: Rega Institute for Medical Research, Katholieke Universiteit Leuven, Minderbroedersstraat 10, B-3000 Louvain, Belgium; 5: Institut für Molekulare Infektionsbiologie, Julius-Maximilians Universität Würzburg, Röntgenring 11, D-97070 Würzburg, Germany
Content Type: Monograph
Publication Year: 2006

Category: Bacterial Pathogenesis

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Identification of Target Proteins of the Lss Secretion System of Corby, Page 1 of 2

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Abstract:

This chapter describes a first putative type I secretion system (Lss) of which is encoded by the locus. In order to identify substrates of this Lss secretion system, the authors performed comparative two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) analysis of extracellular proteins of Corby wild type, Corby lssB mutant, and complemented lssB mutant strain. In this study it was shown that the identified VirK protein of is secreted in an LssB- but not a TatC-dependent manner. Referring to the results, it is implied that the Lss secretion system is also linked to the Lsp type II secretion system in . It is speculated that VirK and p14 are secreted via a concerted action of the Lss and the Lsp system which includes cleavage of the signal sequences during secretion. In and VirK is associated with the vir-regulon, and it was postulated that VirK should have a function in the interaction of the bacteria with the host cells. Therefore, the authors started to generate a mutant strain of Corby and an antibody against VirK to further characterize the expression, secretion, and function of VirK of .

Citation: Albert C, Jacobi S, De Buck E, Lammertyn E, Heuner K. 2006. Identification of Target Proteins of the Lss Secretion System of Corby, p 221-223. 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.ch55
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Identification of Target Proteins of the Lss Secretion System of Legionella pneumophila Corby
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Citation: Albert C, Jacobi S, De Buck E, Lammertyn E, Heuner K. 2006. Identification of Target Proteins of the Lss Secretion System of Corby, p 221-223. 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.ch55
/content/10.1128/9781555815660.ch55.ch55fig01
FIGURE 1
Genomic organization and putative protein function of the locus of . The first line of arrows indicates genes present in the locus. Putative proteins and protein motifs are shown below. DedA, DedA-related protein family; PAP2, type 2 phosphatidic acid phosphatase superfamily.
10.1128/9781555815660/f0222-01_thmb.gif
10.1128/9781555815660/f0222-01.gif
Image of FIGURE 1
FIGURE 1

Genomic organization and putative protein function of the locus of . The first line of arrows indicates genes present in the locus. Putative proteins and protein motifs are shown below. DedA, DedA-related protein family; PAP2, type 2 phosphatidic acid phosphatase superfamily.

Citation: Albert C, Jacobi S, De Buck E, Lammertyn E, Heuner K. 2006. Identification of Target Proteins of the Lss Secretion System of Corby, p 221-223. 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.ch55
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/content/10.1128/9781555815660.ch55.ch55fig02
FIGURE 2
(A) Cutout of comparative analysis of extracellular proteins of Corby wild type and Corby mutant. Proteins of interest were analyzed by mass spectrometry and N-terminal sequencing. (B) Signal sequences of p13 and p14. Arrows mark the putative sites of processing. Amino acids identified by N-terminal sequencing are in bold.
10.1128/9781555815660/f0222-02_thmb.gif
10.1128/9781555815660/f0222-02.gif
Image of FIGURE 2
FIGURE 2

(A) Cutout of comparative analysis of extracellular proteins of Corby wild type and Corby mutant. Proteins of interest were analyzed by mass spectrometry and N-terminal sequencing. (B) Signal sequences of p13 and p14. Arrows mark the putative sites of processing. Amino acids identified by N-terminal sequencing are in bold.

Citation: Albert C, Jacobi S, De Buck E, Lammertyn E, Heuner K. 2006. Identification of Target Proteins of the Lss Secretion System of Corby, p 221-223. 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.ch55
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References

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