楊桃細菌性斑點病菌致病蛋白HrpF生物及生化功能之特性分析

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楊桃細菌性斑點病菌致病蛋白HrpF生物及生化功能之特性分析

Characterization of biological and biochemical functions of the pathogenicity factor HrpF in Pseudomonas syringae pv. averrhoi

黃逸喬 , Ph.D　　Advisor：鄧文玲;黃秀珍　　

繁體中文;英文

楊桃細菌性斑點病菌；第三型分泌系統；第三型分泌系統調控機制； translocon通道蛋白； PAMP誘發免疫反應； hrpF基因； Pseudomonas syringae ； hrpF ； T3SS ； T3SS regulation ； PAMP-triggered immunity ； translocon proteins

Abstract │ Reference (200) │ Altmetrics

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Many Gram-negative phytobacteria often use a syringe-like apparatus called type III secretion system (T3SS) that serves as a dominant pathogenicity factor to directly inject effector proteins into host cells. In Chapter 2, we showed that the hrpF gene of P. syringae pv. averrhoi (Pav), which is located upstream to hrpG, encodes a T3SS-dependent secreted/translocated protein. The hrpF mutant lost the abilities on eliciting disease symptom in its host and hypersensitive response in the nonhost plant, and it was incapable of secreting or translocating the tested T3SS substrates into the bacterial milieu or plant cells. Moreover, overexpressing hrpF in the wild type PavHL1 resulted in delayed HR and reduced t3ss expression. Protein-protein interactions assay was demonstrated that HrpF interacts directly with HrpG and HrpA in vitro and in vivo, and protein stability assays revealed that HrpF assists HrpA stability, which can be reduced by a single amino acid substitution at the 67th lysine residue with alanine, in the bacterial cytoplasm. Thus, HrpF protein acts as a negative factor by binding to HrpG to modulate HrpSVG regulation circuit, and a stabilizer for HrpA pilin by interacting with HrpA to assist the construction of a functional T3SS in the bacteria. Upon translocation, HrpF may act as a virulence factor to promote bacterial parasitism. The possible virulence function of HrpF was analyzed by expressing the dexamethasone-inducible Pav hrpF gene in Arabidopsis thaliana using the Agrobacterium-mediated transformation method. The transgenic plants expressing HrpF were subjected to immunogold labeling and subcellular fractionation analysis for determining its subcellular localization, and immunoprecipitation assays for detecting protein-protein interactions. The results in Chapter 3 showed that HrpF is located on the plant plasma membrane, and it interacts with the translocon proteins HrpZ, HopAK1, and HrpK1. In comparison with the non-transgenic plants, HrpF-expressing plants accumulated less than the average amount of callose elicited by the T3SS-defective nonpathogen hrcC mutant of P. syringae pv. syringae 61. Furthermore, the transgenic plant expressing HrpF restored the T3SS function of P. syringae pv. tomato DC3000 hrpF (hrpFPto) mutant to translocate HopI1Pav-Cya into the plant cells; consequently, infiltration of hrpFPav and hrpFPto mutants into the hrpF-transgenic plants resulted in the respective incompatible and compatible plant responses at the levels equivalent to the ones elicited by the wild-type bacteria.  Based on the results of this study, HrpF is characterized to be a multi-functional protein during P. syringae-plant interactions. The t3ss regulatory circuit starts with the binding of the negative regulator HrpV to HrpS to suppress t3ss expression. Meanwhile, HrpG interacts with HrpF, and HrpF binds to and stabilizes HrpA in the cytoplasm to form a stable protein complex. Upon contacting plant cells, the assembly of T3SS on the cell envelop facilitates the secretion of HrpA and HrpF, shifting the equilibrium of protein interaction from HrpF-HrpG to HrpG-HrpV to release HrpS for subsequent up-regulation of t3ss. When HrpF is translocated via T3SS into the plant cells, it suppresses PTI (pathogen-associated molecular patterns-triggered immunity)-induced defense response, interferes with plant hormones-signaling pathways, and assists the T3SS function to translocate Type III effectors into the plant cells to promote the virulence of P. syringae.

Reference ( 200 ) 〈TOP〉

Abramovitch, R.B., Anderson, J.C. and Martin, G.B. (2006) Bacterial elicitation and evasion of plant innate immunity. Nat. Rev. Mol. Cell Biol. 7, 601-611.
連結：
Abramovitch, R.B. and Martin, G.B. (2004) Strategies used by bacterial pathogens to suppress plant defenses. Curr. Opin. Plant Biol. 7, 356-364.
連結：
(2005) Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol. Microbiol. 56, 54-67.
連結：
Akira, S., Uematsu, S. and Takeuchi, O. (2006) Pathogen recognition and innate immunity. Cell, 124, 783-801.
連結：
Alfano, J.R., Bauer, D.W., Milos, T.M. and Collmer, A. (1996) Analysis of the role of the Pseudomonas syringae pv. syringae HrpZ harpin in elicitation of the hypersensitive response in tobacco using functionally non-polar hrpZ deletion mutations, truncated HrpZ fragments, and hrmA mutations. Mol. Microbiol. 19, 715-728.
連結：

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