Abstract
The Hrp pilus is an indispensable component of type III secretion system, a common virulence factor shared by a number of Gram negative plant pathogens. The type III secretion system enables the bacteria to translocate virulence proteins through the plant cell wall into the plant cytoplasm. The Hrp pilus is a long, up to 5µm, filamentous structure that penetrates the plant cell wall. Expression of the Hrp pili are induced rapidly after transferring bacteria to Hrp inducing minimal medium and also inside the plant tissues. The molecular mechanism of pilus function in the type III secretion system-dependent translocation of proteins remains poorly understood, although it has been suggested that the pilus somehow aids the protein delivery from bacteria into plants. We have studied the expression and assembly of the Hrp pilus, and have shown that the pilus grows by addition of new pilin subunits at the distal end of the filament. Additionally, we have shown that HrpZ protein is secreted from the tip of the pilus. These observations strongly indicate that the Hrp pilus acts as a conduit for secreted proteins, and directs their delivery through the plant cell wall.
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References
Blocker, A., Gounon, P., Larquet, E., Niebuhr, K., Cabiaux, V., Parsot, C., and Sansonetti, P., 1999, The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 147: 683–693.
Brown, I.R., Mansfield, J.W., Taira, S., Roine, E., and Romantschuk, M., 2001, Immunocytochemical localisation of HrpA and HrpZ supports a role for a transfer of effector proteins from Pseudomonas syringae pv. tomato across the plant cell wall. Mol. Plant-Microbe Interact. 14: 394–404.
Casper-Lindley, C., Dahlbeck, D., Clark, E., and Staskawicz, 2002, Direct biochemical evidence for type III secretion-dependent translocation of the AvrBs2 effector protein into plant cells. Proc. Natl. Acad. Sci. USA. 95: 15849–15854.
Dale, C., Plague, G., Wang, B., Ochman, H., and Moran, N., 2002, Type III secretion systems and the evolution of mutualistic endosymbiosis. Proc. Natl. Acad. Sci. USA 99: 12397–12402.
Emerson, S.U., Tokuyasu, K., and Simon, M., 1970, Bacterial flagella: Polarity of elongation. Science 169: 190–192.
Hienonen, E., Roble, E., Romantschuk, M., and Taira, S., 2002, mRNA stability and the secretion signal of HrpA, a pilin secreted by the type III system in Pseudomonas syringae. Mol. Gen. Genomics 266: 973–978.
Hoiczyk, E., and Blobel, G., 2001, Polymerisation of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells. Proc. Natl. Acad. Sci. USA 98: 4669–4674.
Jin, Q., and He, S.Y., 2001, Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae. Science 294: 2556–2558.
Jin, Q., Hu, W., Brown, I., McGhee, G., Hart, P., Jones, A.L. and He, S.Y., 2001, Visualisation of secreted Hrp and Avr proteins along the Hrp pilus during type III secretion in Erwinia amylovora and Pseudomonas syringae. Mol. Microbiol. 40: 1129–1139.
Knutton, S., Rosenshine, I., Pallen, M.J., Nisan, I., Neves, B.C., Bain, C., Wolff, C., Dougan, G., and Frankel, G., 1998, A novel EspA-associated surface organelle of enteropathogenic Escherichia coli involved in protein translocation into epithelial cells. EMBO J. 17: 2166–2176.
Kubori, T., Matsushima, Y., Nakamura, D., Uralil, J., Lara-Tejero, M., Sukhan, A., Galan, J.E., and Aizawa, S.I., 1998, Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280: 602–605.
Leach, J.E., and White, F.F., 1996, Bacterial avirulence proteins. Annu. Rev. Phytopathol. 34: 153–179.
Li, C.-M., Brown, I., Mansfield, J., Stevens, C., Boureau, T., Romantschuk, M., and Taira, S., 2002, Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ. EMBO J. 21: 1909–1915
Misra, T.K., Brown, N.L., Fritzinger, D., Pridmore, R., Barnes, W., and Silver, S., 1984, Mercuric ion-resistance operons of plasmid R100 and transposon Tn501: the beginning of the operon including the regulatory region and the first two structural genes. Proc. Natl. Acad. Sci. U.S.A. 81: 5975–5979.
Roine, E., Wei, W., Yuan, J., Nurmiaho-Lassila, E.L., Kalkkinen, N., Romantschuk, M., and He, S.Y., 1997a, Hrp pilus: an hrp-dependent bacterial surface appendage produced by Pseudomonas syringae pv. tomato DC3000. Proc. Natl. Acad. Sci. USA 94: 3459–3464.
Roine, E., Saarinen, J., Kalkkinen, N., and Romantschuk, M., 1997b, Purified HrpA of Pseudomonas syringae pv. tomato DC3000 reassembles into pili. FEBS Lett. 417: 168–172.
Taira, S., Tuimala, J., Roine, E., Nurmiaho-Lassila, E.L., Savilahti, H., and Romantschuk, M., 1999, Mutational analysis of the Pseudomonas syringae pv. tomato hrpA gene encoding Hrp pilus subunit. Mol. Microbiol. 34: 737–744.
Wei, W., Plovanich-Jones, A., Deng, W.-L., Jin, Q.-L., Collmer, A., Huang, H.-C. and He, S.Y., 2000, The gene coding for the Hrp pilus structural protein is required for type III secretion of Hrp and Avr proteins in Pseudomonas syringae pv. tomato. Proc. Natl. Acad. Sci. USA 97: 2247–2252.
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Li, C.M. et al. (2003). The HRP Pilus of Pseudomonas syringae . In: Iacobellis, N.S., et al. Pseudomonas syringae and related pathogens. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0133-4_30
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DOI: https://doi.org/10.1007/978-94-017-0133-4_30
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-6267-3
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