1887

Chapter 49 : Defining the Translocation Pathway of the Type IV Secretion System

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.

Ebook: Choose a downloadable PDF or ePub file. Chapter is a downloadable PDF file. File must be downloaded within 48 hours of purchase

Buy this Chapter
Digital (?) $15.00

Preview this chapter:
Zoom in
Zoomout

Defining the Translocation Pathway of the Type IV Secretion System, Page 1 of 2

| /docserver/preview/fulltext/10.1128/9781555815660/9781555813901_Chap49-1.gif /docserver/preview/fulltext/10.1128/9781555815660/9781555813901_Chap49-2.gif

Abstract:

The ability of to cause disease is primarily due to its ability to survive inside alveolar macrophages, immune cells capable of destroying most bacteria. The Dot/Icm proteins make up a type IVB secretion system that is required for delivery of multiple protein substrates into the host cell cytoplasm, where they are believed to alter the endocytic pathway and allow the bacterial phagosome to avoid fusion with lysosomal markers. Type IV secretion systems (T4SSs) are used by many pathogens to deliver substrates to host cells, including , , and . The secretion systems used by these pathogens are ancestrally related to plasmid transfer systems and are thus referred to as adapted conjugation systems. Our goal is to characterize the molecular details of how the Dot/Icm secretion complex assembles and functions to export substrates. The approaches to understanding these processes are based on techniques that have proven successful in characterizing the canonical T4SS, the VirB/D4 system from the plant pathogen . To identify functional subcomplexes of the Dot/Icm T4SS, researchers are currently examining protein interactions between Dot/Icm components. One approach researchers are taking to accomplish this is to determine effects on protein stability caused by deletions of other genes. This approach is based on the fact that proteins that interact in a complex often require their interaction partners for stability.

Citation: D. Vincent C, R. Friedman J, P. Vogel J. 2006. Defining the Translocation Pathway of the Type IV Secretion System, p 195-198. 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.ch49

Key Concept Ranking

Type IVB Secretion System
0.4937913
Type IV Secretion Systems
0.46792367
Outer Membrane Proteins
0.40514323
0.4937913
Highlighted Text: Show | Hide
Loading full text...

Full text loading...

Figures

Image of FIGURE 1
FIGURE 1

Subcellular localization of Dot/Icm proteins using Triton X-100 solubility. Cells were grown to early stationary phase and lysed by French press, and membrane proteins were separated from soluble proteins by ultracentrifugation. Inner membrane protein fractions were then extracted with Triton X-100, followed by ultracentrifugation to separate insoluble outer membrane proteins. Shown are Western blots performed with antibodies specific to the proteins listed to the left of each blot. T, total protein; S, soluble protein; M, total membrane protein; I, inner membrane protein; O, outer membrane protein.

Citation: D. Vincent C, R. Friedman J, P. Vogel J. 2006. Defining the Translocation Pathway of the Type IV Secretion System, p 195-198. 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.ch49
Permissions and Reprints Request Permissions
Download as Powerpoint

References

/content/book/10.1128/9781555815660.ch49
1. Buscher, B. A.,, G. M. Conover,, J. L. Miller,, S. A. Vogel,, S. N. Meyers,, R. R. Isberg, and, J. P. Vogel. 2005. The DotL protein, a member of the TraG-coupling protein family, is essential for viability of Legionella pneumophila strain Lp02. J. Bacteriol. 187:29272938.
2. Christie, P. J., and, E. Cascales. 2005. Structural and dynamic properties of bacterial type IV secretion systems (review). Mol. Membr. Biol. 22:5161.
3. Christie, P. J., and, J. P. Vogel. 2000. Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells. Trends Microbiol. 8:354360.
4. Coers, J.,, J. C. Kagan,, M. Matthews,, H. Nagai,, D. M. Zuckman, and, C. R. Roy. 2000. Identification of Icm protein complexes that play distinct roles in the biogenesis of an organelle permissive for Legionella pneumophila intracellular growth. Mol. Microbiol. 38:719736.
5. Dumenil, G., and, R. R. Isberg. 2001. The Legionella pneumophila IcmR protein exhibits chap-erone activity for IcmQ by preventing its participation in high-molecular-weight complexes. Mol. Microbiol. 40:11131127.
6. Hapfelmeier, S.,, N. Domke,, P. C. Zam-bryski, and, C. Baron. 2000. VirB6 is required for stabilization of VirB5 and VirB3 and formation of VirB7 homodimers in Agrobacterium tumefaciens. J. Bacteriol. 182:45054511.
7. Segal, G.,, M. Feldman, and, T. Zusman. 2005. The Icm/Dot type-IV secretion systems of Legionella pneumophila and Coxiella burnetii. FEMS Microbiol. Rev. 29:6581.
8. Sexton, J. A.,, J. S. Pinkner,, R. Roth,, J. E. Heuser,, S. J. Hultgren, and, J. P. Vogel. 2004. The Legionella pneumophila PilT homologue DotB exhibits ATPase activity that is critical for intra-cellular growth. J. Bacteriol. 186:16581666.
9. Sexton, J. A.,, H. J. Yeo, and, J. P. Vogel. 2005. Genetic analysis of the Legionella pneumophila DotB ATPase reveals a role in type IV secretion system protein export. Mol. Microbiol. 57:7084.
10. Yerushalmi, G.,, T. Zusman, and, G. Segal. 2005. Additive effect on intracellular growth by Legionella pneumophila Icm/Dot proteins containing a lipobox motif. Infect. Immun. 73:75787587.

This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error