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Intracellular and Extracellular Phosphatidylinositol 3-Phosphate Produced by Phytophthora Species Is Important for Infection 被引量:7

Intracellular and Extracellular Phosphatidylinositol 3-Phosphate Produced by Phytophthora Species Is Important for Infection
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摘要 RxLR effectors produced by Phytophthora pathogens have been proposed to bind to phosphatidylinositol 3-phosphate (Ptdlns(3)P) to mediate their translocation into host cells and/or to increase their stability in planta. Since the levels of Ptdlns(3)P in plants are low, we examined whether Phytophthora species may produce Ptdlns(3)P to pro- mote infection. We observed that Ptdlns(3)P-specific GFP biosensors could bind to P. parasitica and P. sojae hyphae dur- ing infection of Nicotiana benthamiana leaves transiently secreting the biosensors, suggesting that the hyphae exposed Ptdlns(3)P on their plasma membrane and/or secreted Ptdlns(3)R Silencing of the phosphatidylinositol 3-kinases (PI3K) genes, treatment with LY294002, or expression of Ptdlns(3)pobinding proteins by P. sojae reduced the virulence of the pathogen on soybean, indicating that pathogen-synthesized Ptdlns(3)P was required for full virulence. Secretion of Ptdlns(3)P-binding proteins or of a PI3P-5-kinase by N. benthamiana leaves significantly increased the level of resist- ance to infection by P. parasitica and P. capsici. Together, our results support the hypothesis that Phytophthora species produce external Ptdlns(3)P to aid in infection, such as to promote entry of RxLR effectors into host cells. Our results derived from P. sojae RxLR effector Avrlb confirm that both the N-terminus and the C-terminus of this effector can bind Ptdlns(3)P. RxLR effectors produced by Phytophthora pathogens have been proposed to bind to phosphatidylinositol 3-phosphate (Ptdlns(3)P) to mediate their translocation into host cells and/or to increase their stability in planta. Since the levels of Ptdlns(3)P in plants are low, we examined whether Phytophthora species may produce Ptdlns(3)P to pro- mote infection. We observed that Ptdlns(3)P-specific GFP biosensors could bind to P. parasitica and P. sojae hyphae dur- ing infection of Nicotiana benthamiana leaves transiently secreting the biosensors, suggesting that the hyphae exposed Ptdlns(3)P on their plasma membrane and/or secreted Ptdlns(3)R Silencing of the phosphatidylinositol 3-kinases (PI3K) genes, treatment with LY294002, or expression of Ptdlns(3)pobinding proteins by P. sojae reduced the virulence of the pathogen on soybean, indicating that pathogen-synthesized Ptdlns(3)P was required for full virulence. Secretion of Ptdlns(3)P-binding proteins or of a PI3P-5-kinase by N. benthamiana leaves significantly increased the level of resist- ance to infection by P. parasitica and P. capsici. Together, our results support the hypothesis that Phytophthora species produce external Ptdlns(3)P to aid in infection, such as to promote entry of RxLR effectors into host cells. Our results derived from P. sojae RxLR effector Avrlb confirm that both the N-terminus and the C-terminus of this effector can bind Ptdlns(3)P.
作者 Shan Lu
出处 《Molecular Plant》 SCIE CAS CSCD 2013年第5期1592-1604,共13页 分子植物(英文版)
基金 This work was supported by grants from the National Natural Science Foundation of China (No. 30971889), National Science and Technology Major Projects (No. 2009ZX08005-003B), and the Natural Science Foundation of Jiangsu Province (No. BK2012027).We appreciate Prof. Brett Tyler (Oregon State) for manuscript preparation, and Yuanming Zhang (Nanjing Agricultural University) for suggestions in data analysis. No conflict of interest declared.
关键词 Phytophthora sojae RxLR effectors phosphatidylinositol 3-phosphate (Ptdlns(3)P) phosphatidylinositol3-kinases (PI3Ks). Phytophthora sojae RxLR effectors phosphatidylinositol 3-phosphate (Ptdlns(3)P) phosphatidylinositol3-kinases (PI3Ks).
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  • 1Bhattacharjee, S., Hiller, N.L., liolios, K., Win, J., Kanneganti, T.D., Young, C., Kamoun, S., and Haldar, K. (2006). The malarial hosttargeting signal is conserved in the Irish potato famine pathogen. PLoS Pathog. 2, e50.
  • 2Bhattacharjee, S., Stahelin, R.V., Speicher, K.D., Speicher, D.W., and Haldar, K. (2012). Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell. Cell. 148, 201-212.
  • 3Bos, J.I., Armstrong, M.R., Gilroy, C.M., Boevink, P.C., Hein, I., Taylor, R.M., Zhendong, T., Engelhardt,S., Vetukuri, R.R., Harrower, B., et al. (2010). Phytophthora infestans effector AVR3a is essential for virulence and manipulates plant immunity by stabilizing host E3 ligase CMPG1. Proc. Natl Acad. Sci. U 5 A. 107, 9909-9914.
  • 4Burd, C.G., and Emr, S.D. (1998). Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains. Mol. Cell. 2,157-162.
  • 5Chen, X., Shen, G., Wang, Y., and Zheng, X. (2007). Identification of Phytophthora sojae genes upregulated during the early stage of soybean infection. FEMS Microbiol. Lett. 269, 280-288.
  • 6Clague, M.J., Urbe, S., and de Lartigue, J. (2009). Phosphoinositides and the endocytic pathway. Exp. Cell Res. 315, 1627-1631.
  • 7Dong, S., Qutob, D., Tedman-Jones, J., Kuflu, K., Wang, Y., Tyler, B.M., and Gijzen, M. (2009). The Phytophthora sojae avirulence locus Avr3c encodes a multi-copy RXLR effector with sequence polymorph isms among pathogen strains. PLoS One. 4, e5556.
  • 8Dou, D., Kale, S.D., Wang, X., Chen, Y., Wang, Q., Jiang, R.H., Arredondo, F.D., Anderson, R.G., Thakur, P.B., McDowell, J.M., et al., (2008a). Conserved C-terminal motifs required for avirulence and suppression of cell death by Phytophthora sojae effector Avr1 b. Plant Cell. 20, 1118-1133.
  • 9Dou, D., Kale, S.D., Wang, X., Jiang, R.H., Bruce, N.A., Arredondo, F.D., Zhang, X., and Tyler, B.M. (2008b). RXLR-mediated entry of Phytophthora sojae effector Avrlb into soybean cells does not require pathogen-encoded machinery. Plant Cell. 20, 1930-1947.
  • 10Elison, C., Davidson, K., Anderson, K., Stephens, L.R., and Hawkins, P.T. (2006). Ptdlns3P binding to the PX domain of p40Phox is a physiological signal in NADPH oxidase activation. EMBO J. 25, 4468-4478.

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