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Chapter 56 : Mip: New Function for an Old Protein?

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Abstract:

The macrophage infectivity potentiator (Mip) protein of is one of the most studied proteins and has long been known to promote virulence. Mip protein has been purified and shown to possess peptidyl-prolyl / isomerase (PPI-ase) activity. Comparison of primary structures and crystallographic studies shows that Mip proteins have an N-terminal and a C-terminal domain. Type II secretion is one of five protein secretion systems that can mediate the export of proteins across the gram-negative outer membrane into the extracellular milieu and/or into target cells, and the authors have shown that the type II protein secretion system of is required for optimal replication in macrophages, amoebae, and mice. Interestingly, one of transposon mutants (previously designated NU247) proved to contain a single transposon insertion in the gene, suggesting, for the first time, that Mip might influence protein secretion. This chapter talks about the NU247 reproducibly that showed a 40 to 70% reduction in -NPPC hydrolase activity in its culture supernatants in comparison to the wild-type strain 130b. Since Mip is highly conserved in the genus, and surface and secreted Mip-like proteins are present in other pathogenic microorganisms, Mip and Mip-like proteins might promote the secretion of other important effectors.

Citation: DebRoy S, P. Cianciotto N. 2006. Mip: New Function for an Old Protein?, p 224-227. 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.ch56

Key Concept Ranking

Type II Secretion System
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Figures

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FIGURE 1

Models to explain the impact of Mip on a secreted NPPC hydrolase activity. Initially, like most type II-secreted proteins, the unfolded NPPC hydrolase interacts with components of the Sec system ( ). After the signal peptide is cleaved, the protein is translocated across the inner membrane into the periplasm, where it is folded, possibly with the help of periplasmic chaperones. The protein then interacts with the type II secretion apparatus (Lsp), in order to transit across the outer membrane. At this point, surface-localized Mip may be involved in the final release of active enzyme into the extracellular milieu (). Alternately, Mip might act on newly released protein and, through additional folding (e.g., PPIase) reactions, render it an active enzyme (). Although not depicted here, it is possible that the NPPC hydrolase substrate is translocated across the inner membrane via the twinarginine translocation (Tat) system ( ).

Citation: DebRoy S, P. Cianciotto N. 2006. Mip: New Function for an Old Protein?, p 224-227. 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.ch56
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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. Cianciotto, N. P. 2005. Type II secretion: a protein secretion system for all seasons. Trends Microbiol. 13:581588.
3. Cianciotto, N. P.,, B. I. Eisenstein,, C. H. Mody,, G. B. Toews, and, N. C. Engleberg. 1989. A Legionella pneumophila gene encoding a species-specific surface protein potentiates initiation of in-tracellular infection. Infect. Immun. 57:12551262.
4. Cianciotto, N. P.,, J. Kim Stamos, and, D. W. Kamp. 1995. Infectivity of Legionella pneumophila mip mutant for alveolar epithelial cells. Curr. Microbiol. 30:247250.
5. Doyle, R. M.,, T. W. Steele,, A. M. McLennan,, I. H. Parkinson,, P. A. Manning, and, M. W. Heuzenroeder. 1998. Sequence analysis of the mip gene of the soilborne pathogen Legionella long-beachae. Infect. Immun. 66:14921499.
6. Fischer, G.,, H. Bang,, B. Ludwig,, K. Mann, and, J. Hacker. 1992. Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans iso-merase (PPlase) activity. Mol. Microbiol. 6:13751383.
7. Helbig, J. H.,, P. C. Luck,, M. Steinert,, E. Jacobs, and, M. Witt. 2001. Immunolocalization of the Mip protein of intracellularly and extracellu-larly grown Legionella pneumophila. Lett. Appl. Microbiol. 32:8388.
8. Kohler, R.,, J. Fanghanel,, B. Konig,, E. Lune-berg,, M. Frosch,, J. U. Rahfeld,, R. Hilgenfeld,, G. Fischer,, J. Hacker, and, M. Steinert. 2003. Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila. Infect. Immun. 71:43894397.
9. Ratcliff, R. M.,, S. C. Donnellan,, J. A. Lanser,, P. A. Manning, and, M. W. Heuzenroeder. 1997. Interspecies sequence differences in the Mip protein from the genus Legionella: implications for function and evolutionary relatedness. Mol. Microbiol. 25:11491158.
10. Riboldi-Tunnicliffe, A., B. Konig,, S. Jessen,, M. S. Weiss,, J. Rahfeld,, J. Hacker,, G. Fischer, and, R. Hilgenfeld. 2001. Crystal structure of Mip, a prolylisomerase from Legionella pneumophila. Nat. Struct. Biol. 8:779783.
11. Schmidt, B.,, S. Konig,, D. Svergun,, V. Volkov,, G. Fischer, and, M. H. Koch. 1995. Small-angle X-ray solution scattering study on the dimeriza-tion of the FKBP25mem from Legionella pneumophila. FEBS Lett. 372:169172.
12. Wintermeyer, E.,, B. Ludwig,, M. Steinert,, B. Schmidt,, G. Fischer, and, J. Hacker. 1995. Influence of site specifically altered Mip proteins on intracellular survival of Legionella pneumophila in eukaryotic cells. Infect. Immun. 63:45764583.

Tables

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TABLE 1

Levels of -NPPC hydrolase activity in culture supernatants of wild type 130b and the mutant NU247, carrying the vector pMMB2002 or full-length cloned into pMMB2002 (p.

Citation: DebRoy S, P. Cianciotto N. 2006. Mip: New Function for an Old Protein?, p 224-227. 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.ch56

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