scholarly journals A remorin from Nicotiana benthamiana interacts with the Pseudomonas type-III effector protein HopZ1a and is phosphorylated by the immune-related kinase PBS1

2018 ◽  
Author(s):  
Philip Albers ◽  
Suayib Üstün ◽  
Katja Witzel ◽  
Max Kraner ◽  
Frederik Börnke
Keyword(s):  
Plasma Membrane ◽  
Pseudomonas Syringae ◽  
Nicotiana Benthamiana ◽  
Effector Proteins ◽  
Effector Protein ◽  
Type Iii Effector ◽  
Defense Signaling ◽  
Type Iii ◽  
Transient Overexpression

AbstractThe plasma membrane is at the interface of plant-pathogen interactions and thus many bacterial type-III effector proteins (T3Es) target membrane-associated processes to interfere with immunity. The Pseudomonas syringae T3E is a host cell plasma membrane (PM)-localized effector protein that has several immunity associated host targets but also activates effector triggered immunity (ETI) in resistant backgrounds. Although HopZ1a has been shown to interfere with early defense signaling at the PM, no dedicated plasma membrane-associated HopZ1a target protein has been identified until now. We show here, that HopZ1a interacts with the PM-associated remorin protein NbREM4 from Nicotiana benthamiana in several independent assays. NbREM4 re-localizes to membrane sub-domains after treatment with the bacterial elicitor flg22 and transient overexpression of NbREM4 in N. benthamiana induces the expression of a subset of defense related genes. We can further show that NbREM4 interacts with the immune-related receptor-like cytoplasmic kinase PBS1 and is phosphorylated by PBS1 on several residues in vitro. Thus, we conclude that NbREM4 is associated with early defense signaling at the PM. The possible relevance of the HopZ1a/NbREM4 interaction for HopZ1a virulence and avirulence functions is discussed.

scholarly journals A Remorin from Nicotiana benthamiana Interacts with the Pseudomonas Type-III Effector Protein HopZ1a and is Phosphorylated by the Immune-Related Kinase PBS1

2019 ◽  
Vol 32 (9) ◽  
pp. 1229-1242 ◽  
Author(s):  
Philip Albers ◽  
Suayib Üstün ◽  
Katja Witzel ◽  
Max Kraner ◽  
Frederik Börnke
Keyword(s):  
Pseudomonas Syringae ◽  
Nicotiana Benthamiana ◽  
Effector Protein ◽  
Type Iii Effector ◽  
Defense Signaling ◽  
Type Iii ◽  
Target Membrane ◽  
Effector Triggered Immunity ◽  
Transient Overexpression

The plasma membrane (PM) is at the interface of plant–pathogen interactions and, thus, many bacterial type-III effector (T3E) proteins target membrane-associated processes to interfere with immunity. The Pseudomonas syringae T3E HopZ1a is a host cell PM-localized effector protein that has several immunity-associated host targets but also activates effector-triggered immunity in resistant backgrounds. Although HopZ1a has been shown to interfere with early defense signaling at the PM, no dedicated PM-associated HopZ1a target protein has been identified until now. Here, we show that HopZ1a interacts with the PM-associated remorin protein NbREM4 from Nicotiana benthamiana in several independent assays. NbREM4 relocalizes to membrane nanodomains after treatment with the bacterial elicitor flg22 and transient overexpression of NbREM4 in N. benthamiana induces the expression of a subset of defense-related genes. We can further show that NbREM4 interacts with the immune-related receptor-like cytoplasmic kinase avrPphB-susceptible 1 (PBS1) and is phosphorylated by PBS1 on several residues in vitro. Thus, we conclude that NbREM4 is associated with early defense signaling at the PM. The possible relevance of the HopZ1a–NbREM4 interaction for HopZ1a virulence and avirulence functions is discussed. [Formula: see text]Copyright © 2019 The Author(s). This is an open access article distributed under the CC BY-NC-ND 4.0 International license .

scholarly journals Eukaryotic Fatty Acylation Drives Plasma Membrane Targeting and Enhances Function of Several Type III Effector Proteins from Pseudomonas syringae

Cell ◽  
2000 ◽  
Vol 101 (4) ◽  
pp. 353-363 ◽  
Author(s):  
Zachary Nimchuk ◽  
Eric Marois ◽  
Susanne Kjemtrup ◽  
R.Todd Leister ◽  
Fumiaki Katagiri ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Pseudomonas Syringae ◽  
Effector Proteins ◽  
Membrane Targeting ◽  
Type Iii Effector ◽  
Type Iii ◽  
Fatty Acylation

scholarly journals Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease

2003 ◽  
Vol 49 (6) ◽  
pp. 1537-1546 ◽  
Author(s):  
Michael J. Axtell ◽  
Stephen T. Chisholm ◽  
Douglas Dahlbeck ◽  
Brian J. Staskawicz
Keyword(s):  
Pseudomonas Syringae ◽  
Cysteine Protease ◽  
Molecular Evidence ◽  
Effector Protein ◽  
Type Iii Effector ◽  
Type Iii

scholarly journals A Pseudomonas syringae pv. tomato DC3000 mutant lacking the type III effector HopQ1-1 is able to cause disease in the model plant Nicotiana benthamiana

2007 ◽  
Vol 51 (1) ◽  
pp. 32-46 ◽  
Author(s):  
Chia-Fong Wei ◽  
Brian H. Kvitko ◽  
Rena Shimizu ◽  
Emerson Crabill ◽  
James R. Alfano ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Nicotiana Benthamiana ◽  
Tomato Dc3000 ◽  
Type Iii Effector ◽  
Model Plant ◽  
Type Iii

Distribution of espI among clinical enterohaemorrhagic and enteropathogenic Escherichia coli isolates

2004 ◽  
Vol 53 (11) ◽  
pp. 1145-1149 ◽  
Author(s):  
Rosanna Mundy ◽  
Claire Jenkins ◽  
Jun Yu ◽  
Henry Smith ◽  
Gad Frankel
Keyword(s):  
Escherichia Coli ◽  
Type Iii Secretion ◽  
Severe Disease ◽  
Pathogenicity Island ◽  
Effector Proteins ◽  
Effector Protein ◽  
Enteropathogenic Escherichia Coli ◽  
Type Iii Effector ◽  
Type Iii

Enterohaemorrhagic (EHEC) and enteropathogenic (EPEC) Escherichia coli are important diarrhoeagenic pathogens; infection is dependent on translocation of a number of type III effector proteins. Until recently all the known effectors were encoded on the LEE pathogenicity island, which also encodes the adhesin intimin and the type III secretion apparatus. Recently, a novel non-LEE effector protein, EspI/NleA, which is required for full virulence in vivo and is encoded on a prophage, was identified. The aim of this study was to determine the distribution of espI among clinical EHEC and EPEC isolates. espI was detected in 86 % and 53 % of LEE+ EHEC and EPEC strains, respectively. Moreover, the espI gene was more commonly found in patients suffering from a more severe disease.

scholarly journals Immunocytochemical Localization of HrpA and HrpZ Supports a Role for the Hrp Pilus in the Transfer of Effector Proteins from Pseudomonas syringae pv. tomato Across the Host Plant Cell Wall

2001 ◽  
Vol 14 (3) ◽  
pp. 394-404 ◽  
Author(s):  
Ian R. Brown ◽  
John W. Mansfield ◽  
Suvi Taira ◽  
Elina Roine ◽  
Martin Romantschuk
Keyword(s):  
Cell Wall ◽  
Pseudomonas Syringae ◽  
Plant Cell ◽  
Type Iii Secretion ◽  
Plant Cell Wall ◽  
Immunogold Labeling ◽  
Effector Proteins ◽  
Basal Bodies ◽  
Type Iii

The Hrp pilus, composed of HrpA subunits, is an essential component of the type III secretion system in Pseudomonas syringae. We used electron microscopy (EM) and immunocytochemistry to examine production of the pilus in vitro from P. syringae pv. tomato strain DC3000 grown under hrp-inducing conditions on EM grids. Pili, when labeled with antibodies to HrpA, developed rapidly in a nonpolar manner shortly after the detection of the hrpA transcript and extended up to 5 μm into surrounding media. Structures at the base of the pilus were clearly differentiated from the basal bodies of flagella. The HrpZ protein, also secreted via the type III system, was found by immunogold labeling to be associated with the pilus in vitro. Accumulation and secretion of HrpA and HrpZ were also examined quantitatively after the inoculation of wild-type DC3000 and hrpA and hrpZ mutants into leaves of Arabidopsis thaliana. The functional pilus crossed the plant cell wall to generate tracks of immunogold labeling for HrpA and HrpZ. Mutants that produced HrpA but did not assemble pili were nonpathogenic, did not secrete HrpA protein, and were compromised for the accumulation of HrpZ. A model is proposed in which the rapidly elongating Hrp pilus acts as a moving conveyor, facilitating transfer of effector proteins from bacteria to the plant cytoplasm across the formidable barrier of the plant cell wall.

scholarly journals The Type III Effector NleD from Enteropathogenic Escherichia coli Differentiates between Host Substrates p38 and JNK

2016 ◽  
Vol 85 (2) ◽  
Author(s):  
Kristina Creuzburg ◽  
Cristina Giogha ◽  
Tania Wong Fok Lung ◽  
Nichollas E. Scott ◽  
Sabrina Mühlen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Effector Proteins ◽  
Mitogen Activated Protein Kinase ◽  
Mass Spectrometry Analysis ◽  
Single Amino Acid ◽  
Luciferase Reporter ◽  
Type Iii Effector ◽  
Type Iii ◽  
Infected Cells

ABSTRACT Enteropathogenic Escherichia coli (EPEC) is a gastrointestinal pathogen that utilizes a type III secretion system (T3SS) to inject an array of virulence effector proteins into host enterocytes to subvert numerous cellular processes for successful colonization and dissemination. The T3SS effector NleD is a 26-kDa zinc metalloprotease that is translocated into host enterocytes, where it directly cleaves and inactivates the mitogen-activated protein kinase signaling proteins JNK and p38. Here a library of 91 random transposon-based, in-frame, linker insertion mutants of NleD were tested for their ability to cleave JNK and p38 during transient transfection of cultured epithelial cells. Immunoblot analysis of p38 and JNK cleavage showed that 7 mutant derivatives of NleD no longer cleaved p38 but maintained the ability to cleave JNK. Site-directed mutation of specific regions surrounding the insertion sites within NleD revealed that a single amino acid, R203, was essential for cleavage of p38 but not JNK in a direct in vitro cleavage assay, in transiently transfected cells, or in EPEC-infected cells. Mass spectrometry analysis narrowed the cleavage region to within residues 187 and 213 of p38. Mutation of residue R203 within NleD to a glutamate residue abolished the cleavage of p38 and impaired the ability of NleD to inhibit AP-1-dependent gene transcription of a luciferase reporter. Furthermore, the R203 mutation abrogated the ability of NleD to dampen interleukin-6 production in EPEC-infected cells. Overall, this work provides greater insight into substrate recognition and specificity by the type III effector NleD.

scholarly journals Pseudomonas Type III Effector AvrPto Suppresses the Programmed Cell Death Induced by Two Nonhost Pathogens in Nicotiana benthamiana and Tomato

2004 ◽  
Vol 17 (12) ◽  
pp. 1328-1336 ◽  
Author(s):  
Li Kang ◽  
Xiaoyan Tang ◽  
Kirankumar S. Mysore
Keyword(s):  
Cell Death ◽  
Disease Resistance ◽  
Programmed Cell Death ◽  
Pseudomonas Syringae ◽  
Type Iii Secretion ◽  
Nicotiana Benthamiana ◽  
Effector Proteins ◽  
Type Iii ◽  
Bacterial Pathogenicity ◽  
Suppression Effects

Many gram-negative bacterial pathogens rely on a type III secretion system to deliver a number of effector proteins into the host cell. Though a number of these effectors have been shown to contribute to bacterial pathogenicity, their functions remain elusive. Here we report that AvrPto, an effector known for its ability to interact with Pto and induce Pto-mediated disease resistance, inhibited the hypersensitive response (HR) induced by nonhost pathogen interactions. Pseudomonas syringae pv. tomato T1 causes an HR-like cell death on Nicotiana benthamiana. This rapid cell death was delayed significantly in plants inoculated with P. syringae pv. tomato expressing avrPto. In addition, P. syringae pv. tabaci expressing avrPto suppressed nonhost HR on tomato prf3 and ptoS lines. Transient expression of avrPto in both N. benthamiana and tomato prf3 plants also was able to suppress nonhost HR. Interestingly, AvrPto failed to suppress cell death caused by other elicitors and nonhost pathogens. AvrPto also failed to suppress cell death caused by certain gene-for-gene disease resistance interactions. Experiments with avrPto mutants revealed several residues important for the suppression effects. AvrPto mutants G2A, G99V, P146L, and a 12-amino-acid C-terminal deletion mutant partially lost the suppression ability, whereas S94P and I96T enhanced suppression of cell death in N. benthamiana. These results, together with other discoveries, demonstrated that suppression of host-programmed cell death may serve as one of the strategies bacterial pathoens use for successful invasion.

scholarly journals The type III effector HopF2Pto targets Arabidopsis RIN4 protein to promote Pseudomonas syringae virulence

2010 ◽  
Vol 107 (5) ◽  
pp. 2349-2354 ◽  
Author(s):  
Mike Wilton ◽  
Rajagopal Subramaniam ◽  
James Elmore ◽  
Corinna Felsensteiner ◽  
Gitta Coaker ◽  
...  
Keyword(s):  
Pseudomonas Syringae ◽  
Plant Immunity ◽  
Effector Proteins ◽  
Type Iii ◽  
Pathogen Effector ◽  
Effector Triggered Immunity ◽  
Type Iii Secretion Effector ◽  
Virulence Target

Plant immunity can be induced by two major classes of pathogen-associated molecules. Pathogen- or microbe-associated molecular patterns (PAMPs or MAMPs) are conserved molecular components of microbes that serve as “non-self” features to induce PAMP-triggered immunity (PTI). Pathogen effector proteins used to promote virulence can also be recognized as “non-self” features or induce a “modified-self” state that can induce effector-triggered immunity (ETI). The Arabidopsis protein RIN4 plays an important role in both branches of plant immunity. Three unrelated type III secretion effector (TTSE) proteins from the phytopathogen Pseudomonas syringae, AvrRpm1, AvrRpt2, and AvrB, target RIN4, resulting in ETI that effectively restricts pathogen growth. However, no pathogenic advantage has been demonstrated for RIN4 manipulation by these TTSEs. Here, we show that the TTSE HopF2Pto also targets Arabidopsis RIN4. Transgenic plants conditionally expressing HopF2Pto were compromised for AvrRpt2-induced RIN4 modification and associated ETI. HopF2Pto interfered with AvrRpt2-induced RIN4 modification in vitro but not with AvrRpt2 activation, suggestive of RIN4 targeting by HopF2Pto. In support of this hypothesis, HopF2Pto interacted with RIN4 in vitro and in vivo. Unlike AvrRpm1, AvrRpt2, and AvrB, HopF2Pto did not induce ETI and instead promoted P. syringae growth in Arabidopsis. This virulence activity was not observed in plants genetically lacking RIN4. These data provide evidence that RIN4 is a major virulence target of HopF2Pto and that a pathogenic advantage can be conveyed by TTSEs that target RIN4.

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