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Cell Host and Microbe - Phytopathogen Effectors Subverting Host Immunity: Different Foes, Similar Battleground

Cell Host and Microbe - Phytopathogen Effectors Subverting Host Immunity: Different Foes, Similar Battleground | Plant-microbe interaction | Scoop.it

Phytopathogenic bacteria, fungi, and oomycetes invade and colonize their host plants through distinct routes. These pathogens secrete diverse groups of effector proteins that aid infection and establishment of different parasitic lifestyles. Despite this diversity, a comparison of different plant-pathogen systems has revealed remarkable similarities in the host immune pathways targeted by effectors from distinct pathogen groups. Immune signaling pathways mediated by pattern recognition receptors, phytohormone homeostasis or signaling, defenses associated with host secretory pathways and pathogen penetrations, and plant cell death represent some of the key processes controlling disease resistance against diverse pathogens. These immune pathways are targeted by effectors that carry a wide range of biochemical functions and are secreted by completely different pathogen groups, suggesting that these pathways are a common battleground encountered by many plant pathogens.

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Plant-microbe interaction
Current research on plant immunity, effector proteins, and other inspiring articles
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Frontiers | Interactions of Xanthomonas type-III effector proteins with the plant ubiquitin and ubiquitin-like pathways | Plant-Microbe Interaction

Frontiers | Interactions of Xanthomonas type-III effector proteins with the plant ubiquitin and ubiquitin-like pathways | Plant-Microbe Interaction | Plant-microbe interaction | Scoop.it
In eukaryotes, regulated protein turnover is required during many cellular processes, including defense against pathogens. Ubiquitination and degradation of ubiquitinated proteins via the ubiquitin – proteasome system (UPS) is the main pathway for the turnover of intracellular proteins in eukaryotes. The extensive utilization of the UPS in host cells makes it an ideal pivot for the manipulation of cellular processes by pathogens. Like many other Gram-negative bacteria, Xanthomonas species secrete a suite of type-III effector proteins (T3Es) into their host cells to promote virulence. Some of these T3Es exploit the plant UPS to interfere with immunity. This review summarizes T3E examples from the genus Xanthomonas with a proven or suggested interaction with the host UPS or UPS-like systems and also discusses the apparent paradox that arises from the presence of T3Es that inhibit the UPS in general while others rely on its activity for their function.
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My first Review is online! Also first paper in Frontiers in Plant Science. Next one in this issue is following soon...

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The Pseudomonas syringae Type III Effector HopF2 Suppresses Arabidopsis Stomatal Immunity

The Pseudomonas syringae Type III Effector HopF2 Suppresses Arabidopsis Stomatal Immunity | Plant-microbe interaction | Scoop.it

Pseudomonas syringae subverts plant immune signalling through injection of type III secreted effectors (T3SE) into host cells. The T3SE HopF2 can disable Arabidopsis immunity through Its ADP-ribosyltransferase activity. Proteomic analysis of HopF2 interacting proteins identified a protein complex containing ATPases required for regulating stomatal aperture, suggesting HopF2 may manipulate stomatal immunity. Here we report HopF2 can inhibit stomatal immunity independent of its ADP-ribosyltransferase activity. Transgenic expression of HopF2 in Arabidopsis inhibits stomatal closing in response to P. syringae and increases the virulence of surface inoculated P. syringae. Further, transgenic expression of HopF2 inhibits flg22 induced reactive oxygen species production. Intriguingly, ADP-ribosyltransferase activity is dispensable for inhibiting stomatal immunity and flg22 induced reactive oxygen species. Together, this implies HopF2 may be a bifunctional T3SE with ADP-ribosyltransferase activity required for inhibiting apoplastic immunity and an independent function required to inhibit stomatal immunity.

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Pepper Heat Shock Protein 70a Interacts with the Type III Effector AvrBsT and Triggers Plant Cell Death and Immunity

Pepper Heat Shock Protein 70a Interacts with the Type III Effector AvrBsT and Triggers Plant Cell Death and Immunity | Plant-microbe interaction | Scoop.it
Heat shock proteins (HSPs) function as molecular chaperones and are essential for the maintenance and/or restoration of protein homeostasis. The Xanthomonas type III effector AvrBsT induces hypersensitive cell death in pepper (Capsicum annuum). Here, we report the identification of the pepper CaHSP70a as an AvrBsT-interacting protein. Bimolecular fluorescence complementation and co-immunoprecipitation assays confirm the specific interaction between CaHSP70a and AvrBsT in planta. The CaHSP70a peptide-binding domain is essential for its interaction with AvrBsT. Heat stress (37°C) and Xanthomonas campestris pv. vesicatoria (Xcv) infection distinctly induce CaHSP70a in pepper leaves. Cytoplasmic CaHSP70a proteins significantly accumulate in pepper leaves to induce the hypersensitive cell death response by Xcv (avrBsT) infection. Transient CaHSP70a overexpression induces hypersensitive cell death under heat stress, which is accompanied by strong induction of defense- and cell death-related genes. CaHSP70a peptide-binding domain and ATPase-binding domain are required to trigger cell death under heat stress. Transient co-expression of CaHSP70a and avrBsT leads to cytoplasmic localization of the CaHSP70a-AvrBsT complex, and significantly enhances avrBsT-triggered cell death in Nicotiana benthamiana. CaHSP70a silencing in pepper enhances Xcv growth, but disrupts the reactive oxygen species burst and cell death response during Xcv infection. Expression of some defense marker genes is significantly reduced in CaHSP70a-silenced leaves, with lower levels of the defense hormones salicylic acid and jasmonic acid. Together, these results suggest that CaHSP70a interacts with the type III effector AvrBsT and is required for cell death and immunity in plants.
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Mitogen-activated protein kinase 6 regulates NPR1 gene expression and activation during leaf senescence induced by salicylic acid

Mitogen-activated protein kinase 6 regulates NPR1 gene expression and activation during leaf senescence induced by salicylic acid | Plant-microbe interaction | Scoop.it
Plant senescence is a highly regulated process that can be induced by a range of factors. The nonexpressor of pathogenesis-related genes 1 (npr1) mutant is defective in the salicylic acid (SA) signalling pathway, displaying delayed yellowing during developmental senescence. However, the regulating mechanism of NPR1 on exogenous SA-induced senescence in detached Arabidopsis leaves has not yet been clarified. It was shown here that mitogen-activated protein kinase 6 (MPK6) is involved in promoting exogenous SA-induced detached leaf senescence. During the process of SA-induced senescence, the expression of NPR1 and senescence-related transcription factor WRKY6 was suppressed in mpk6 mutant plants. Further analyses showed that the NPR1 mRNA level is reduced in wrky6 mutants and enhanced in WRKY6 overexpressing lines. Meanwhile, chromatin immunoprecipitation experiments revealed that WRKY6 binds directly to the NPR1 promoter containing W-box motifs. Moreover, inhibition of MPK6 function diminished SA-induced monomerization and nuclear localization of NPR1. In addition, the expression of Trx h5, which catalyses the SA-induced NPR1 activation, was suppressed in the mpk6 mutant, suggesting that MPK6 promotes NPR1 activation, possibly by regulating the expression of Trx h5. Collectively, MPK6-mediated WRKY6 and Trx h5 transcriptional activation co-regulated the expression of the NPR1 gene and the monomerization of NPR1 protein, allowing it to enter the nucleus, thereby promoting SA-induced leaf senescence. These results provide new insight into the mechanism of exogenous SA-induced detached leaf senescence.

Via Christophe Jacquet
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The Plasmodesmal Protein PDLP1 Localises to Haustoria-Associated Membranes during Downy Mildew Infection and Regulates Callose Deposition

The Plasmodesmal Protein PDLP1 Localises to Haustoria-Associated Membranes during Downy Mildew Infection and Regulates Callose Deposition | Plant-microbe interaction | Scoop.it
The downy mildew pathogen Hyaloperonospora arabidopsidis (Hpa) is a filamentous oomycete that invades plant cells via sophisticated but poorly understood structures called haustoria. Haustoria are separated from the host cell cytoplasm and surrounded by an extrahaustorial membrane (EHM) of unknown origin. In some interactions, including Hpa-Arabidopsis, haustoria are progressively encased by host-derived, callose-rich materials but the molecular mechanisms by which callose accumulates around haustoria remain unclear. Here, we report that PLASMODESMATA-LOCATED PROTEIN 1 (PDLP1) is expressed at high levels in Hpa infected cells. Unlike other plasma membrane proteins, which are often excluded from the EHM, PDLP1 is located at the EHM in Hpa-infected cells prior to encasement. The transmembrane domain and cytoplasmic tail of PDLP1 are sufficient to convey this localization. PDLP1 also associates with the developing encasement but this association is lost when encasements are fully mature. We found that the pdlp1,2,3 triple mutant is more susceptible to Hpa while overexpression of PDLP1 enhances plant resistance, suggesting that PDLPs enhance basal immunity against Hpa. Haustorial encasements are depleted in callose in pdlp1,2,3 mutant plants whereas PDLP1 over-expression elevates callose deposition around haustoria and across the cell surface. These data indicate that PDLPs contribute to callose encasement of Hpa haustoria and suggests that the deposition of callose at haustoria may involve similar mechanisms to callose deposition at plasmodesmata.
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Bacterial effector modulation of host E3 ligase activity suppresses PAMP-triggered immunity in rice : Nature Communications : Nature Publishing Group

Pathogen effector proteins are delivered to host cells to suppress plant immunity. However, the mechanisms by which effector proteins function are largely unknown. Here we show that expression of XopPXoo, an effector of rice pathogen Xanthomonas oryzae pv. oryzae, in rice strongly suppresses peptidoglycan (PGN)- and chitin-triggered immunity and resistance to X. oryzae. XopPXoo targets OsPUB44, a rice ubiquitin E3 ligase with a unique U-box domain. We find that XopPXoo directly interacts with the OsPUB44 U-box domain and inhibits ligase activity. Two amino-acid residues specific for the OsPUB44 U-box domain are identified, which are responsible for the interaction with XopPXoo. Silencing of OsPUB44 suppresses PGN- and chitin-triggered immunity and X. oryzae resistance, indicating that OsPUB44 positively regulates immune responses. Thus, it is likely that XopPXoo suppresses immune responses by directly interacting with and inhibiting a positive regulator of plant immunity.
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Trade-off between growth and immunity: role of brassinosteroids

Trade-off between growth and immunity: role of brassinosteroids | Plant-microbe interaction | Scoop.it

Highlights•

Brassinosteroids (BR) regulate the growth-immunity trade-off in Arabidopsis.

The co-receptor BAK1 is not rate-limiting between the BR and immune pathways.

The BR-activated transcription factor BZR1 is a master regulator of this trade-off.

BZR1 and HBI1 form a core transcriptional cascade and regulatory hub.

The effects of BR on plant–pathogen interactions require further investigation.

A balance between growth and immunity exists in plants. Recently, the growth-promoting hormones brassinosteroids (BR) have emerged as crucial regulators of the growth-immunity trade-off, although the molecular mechanisms underlying this role remained unclear. New evidence obtained from the model plant Arabidopsis thaliana points at an indirect crosstalk between BR signaling and immunity, mediated by the transcription factors BZR1 and HBI1, which suppress immunity upon BR perception. The core transcriptional cascade formed by BZR1 and HBI1 seems to act as a regulatory hub on which multiple signaling inputs impinge, ensuring effective fine-tuning of the trade-off between growth and immunity in a timely and cost-efficient manner.


Via Christophe Jacquet
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Light intensity and temperature affect systemic spread of silencing signal in transient agroinfiltration studies

Light intensity and temperature affect systemic spread of silencing signal in transient agroinfiltration studies | Plant-microbe interaction | Scoop.it

RNA silencing is a sequence-specific post-transcriptional gene inactivation mechanism that operates in diverse organisms and that can extend beyond its site of initiation, owing to the movement of the silencing signal, called non-autonomous gene silencing. Previous studies have shown that several factors manifest the movement of the silencing signal, such as the size (21 or 24 nucleotides) of the secondary small interfering RNA (siRNA) produced, the steady-state concentration of siRNAs and their cognate messenger RNA (mRNA) or a change in the sink–source status of plant parts affecting phloem translocation. Our study shows that both light intensity and temperature have a significant impact on the systemic movement of the silencing signal in transient agroinfiltration studies in Nicotiana benthamiana. At higher light intensities (≥450 μE/m2/s) and higher temperatures (≥30 °C), gene silencing was localized to leaf tissue that was infiltrated, without any systemic spread. Interestingly, in these light and temperature conditions (≥450 μE/m2/s and ≥30 °C), the N. benthamiana plants showed recovery from the viral symptoms. However, the reduced systemic silencing and reduced viral symptom severity at higher light intensities were caused by a change in the sink–source status of the plant, ultimately affecting the phloem translocation of small RNAs or the viral genome. In contrast, at lower light intensities (<300 μE/m2/s) with a constant temperature of 25 °C, there was strong systemic movement of the silencing signal in the N. benthamiana plants and reduced recovery from virus infections. The accumulation of gene-specific siRNAs was reduced at higher temperature as a result of a reduction in the accumulation of transcript on transient agroinfiltration of RNA interference (RNAi) constructs, mostly because of poor T-DNA transfer activity of Agrobacterium, possibly also accompanied by reduced phloem translocation.

 

 


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PLOS Genetics: The Nuclear Immune Receptor RPS4 Is Required for RRS1SLH1-Dependent Constitutive Defense Activation in Arabidopsis thaliana (2014)

PLOS Genetics: The Nuclear Immune Receptor RPS4 Is Required for RRS1SLH1-Dependent Constitutive Defense Activation in Arabidopsis thaliana (2014) | Plant-microbe interaction | Scoop.it

Plant nucleotide-binding leucine-rich repeat (NB-LRR) disease resistance (R) proteins recognize specific “avirulent” pathogen effectors and activate immune responses. NB-LRR proteins structurally and functionally resemble mammalian Nod-like receptors (NLRs). How NB-LRR and NLR proteins activate defense is poorly understood. The divergently transcribed Arabidopsis R genes, RPS4 (resistance to Pseudomonas syringae 4) and RRS1 (resistance to Ralstonia solanacearum 1), function together to confer recognition of PseudomonasAvrRps4 and Ralstonia PopP2. RRS1 is the only known recessive NB-LRR R gene and encodes a WRKY DNA binding domain, prompting suggestions that it acts downstream of RPS4 for transcriptional activation of defense genes. We define here the early RRS1-dependent transcriptional changes upon delivery of PopP2 via Pseudomonas type III secretion. The Arabidopsis slh1 (sensitive to low humidity 1) mutant encodes an RRS1 allele (RRS1SLH1) with a single amino acid (leucine) insertion in the WRKY DNA-binding domain. Its poor growth due to constitutive defense activation is rescued at higher temperature. Transcription profiling data indicate that RRS1SLH1-mediated defense activation overlaps substantially with AvrRps4- and PopP2-regulated responses. To better understand the genetic basis of RPS4/RRS1-dependent immunity, we performed a genetic screen to identify suppressor of slh1 immunity (sushi) mutants. We show that many sushi mutants carry mutations in RPS4, suggesting that RPS4 acts downstream or in a complex with RRS1. Interestingly, several mutations were identified in a domain C-terminal to the RPS4 LRR domain. Using an Agrobacterium-mediated transient assay system, we demonstrate that the P-loop motif of RPS4 but not of RRS1SLH1 is required for RRS1SLH1 function. We also recapitulate the dominant suppression of RRS1SLH1 defense activation by wild type RRS1 and show this suppression requires an intact RRS1 P-loop. These analyses of RRS1SLH1shed new light on mechanisms by which NB-LRR protein pairs activate defense signaling, or are held inactive in the absence of a pathogen effector.


Via Kamoun Lab @ TSL, CP
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Frontiers | Sustained mitogen-activated protein kinase activation reprograms defense metabolism and phosphoprotein profile in Arabidopsis thaliana | Plant Proteomics

Mitogen-activated protein kinases (MAPKs) target a variety of protein substrates to regulate cellular signaling processes in eukaryotes. In plants, the number of identified MAPK substrates that control plant defense responses is still limited. Here, we generated transgenic Arabidopsis thaliana plants with an inducible system to simulate in vivo activation of two stress-activated MAPKs, MPK3 and MPK6. Metabolome analysis revealed that this artificial MPK3/6 activation (without any exposure to pathogens or other stresses) is sufficient to drive the production of major defense-related metabolites, including various camalexin, indole glucosinolate and agmatine derivatives. An accompanying (phospho)proteome analysis led to detection of hundreds of potential phosphoproteins downstream of MPK3/6 activation. Besides known MAPK substrates, many candidates on this list possess typical MAPK-targeted phosphosites and in many cases, the corresponding phosphopeptides were detected by mass spectrometry. Notably, several of these putative phosphoproteins have been reported to be associated with the biosynthesis of antimicrobial defense substances (e.g. WRKY transcription factors and proteins encoded by the genes from the “PEN” pathway required for penetration resistance to filamentous pathogens). Thus, this work provides an inventory of candidate phosphoproteins, including putative direct MAPK substrates, for future analysis of MAPK-mediated defense control. (Proteomics data are available with the identifier PXD001252 via ProteomeXchange, http://proteomecentral.proteomexchange.org).
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A Unique Plant ESCRT Component, FREE1, Regulates Multivesicular Body Protein Sorting and Plant Growth: Current Biology

A Unique Plant ESCRT Component, FREE1, Regulates Multivesicular Body Protein Sorting and Plant Growth: Current Biology | Plant-microbe interaction | Scoop.it
Highlights•FREE1 is a plant-specific and PVC-localized FYVE domain protein binding to PI3P•FREE1 is in a complex with ESCRT-I via a direct interaction with Vps23•FREE1 directly binds to ubiquitin and regulates vacuolar membrane protein sorting•FREE1 is essential for PVC/MVB biogenesis and plant growthSummary

Tight control of membrane protein homeostasis by selective degradation is crucial for proper cell signaling and multicellular organismal development. Membrane proteins destined for degradation, such as misfolded proteins or activated receptors, are usually ubiquitinated and sorted into the intraluminal vesicles (ILVs) of prevacuolar compartments/multivesicular bodies (PVCs/MVBs), which then fuse with vacuoles/lysosomes to deliver their contents to the lumen for degradation by luminal proteases [ 1 ]. The formation of ILVs and the sorting of ubiquitinated membrane cargoes into them are facilitated by the endosomal sorting complex required for transport (ESCRT) machinery [ 2–4 ]. Plants possess most evolutionarily conserved members of the ESCRT machinery but apparently lack orthologs of ESCRT-0 subunits and the ESCRT-I component Mvb12 [ 5–8 ]. Here, we identified a unique plant ESCRT component called FYVE domain protein required for endosomal sorting 1 (FREE1). FREE1 binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin and specifically interacts with Vps23 via PTAP-like tetrapeptide motifs to be incorporated into the ESCRT-I complex. Arabidopsis free1 mutant is seedling lethal and defective in the formation of ILVs in MVBs. Consequently, endocytosed plasma membrane (PM) proteins destined for degradation, such as the auxin efflux carrier PIN2 [ 9, 10 ], cannot reach the lumen of the vacuole and mislocalize to the tonoplast. Collectively, our findings provide the first functional characterization of a plant FYVE domain protein, which is essential for plant growth via its role as a unique evolutionary ESCRT component for MVB biogenesis and vacuolar sorting of membrane proteins.

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Expression Profiling during Arabidopsis/Downy Mildew Interaction Reveals a Highly-Expressed Effector That Attenuates Responses to Salicylic Acid

Expression Profiling during Arabidopsis/Downy Mildew Interaction Reveals a Highly-Expressed Effector That Attenuates Responses to Salicylic Acid | Plant-microbe interaction | Scoop.it
Plants have evolved strong innate immunity mechanisms, but successful pathogens evade or suppress plant immunity via effectors delivered into the plant cell. Hyaloperonospora arabidopsidis (Hpa) causes downy mildew on Arabidopsis thaliana, and a genome sequence is available for isolate Emoy2. Here, we exploit the availability of genome sequences for Hpa and Arabidopsis to measure gene-expression changes in both Hpa and Arabidopsis simultaneously during infection. Using a high-throughput cDNA tag sequencing method, we reveal expression patterns of Hpa predicted effectors and Arabidopsis genes in compatible and incompatible interactions, and promoter elements associated with Hpa genes expressed during infection. By resequencing Hpa isolate Waco9, we found it evades Arabidopsis resistance gene RPP1 through deletion of the cognate recognized effector ATR1. Arabidopsis salicylic acid (SA)-responsive genes including PR1 were activated not only at early time points in the incompatible interaction but also at late time points in the compatible interaction. By histochemical analysis, we found that Hpa suppresses SA-inducible PR1 expression, specifically in the haustoriated cells into which host-translocated effectors are delivered, but not in non-haustoriated adjacent cells. Finally, we found a highly-expressed Hpa effector candidate that suppresses responsiveness to SA. As this approach can be easily applied to host-pathogen interactions for which both host and pathogen genome sequences are available, this work opens the door towards transcriptome studies in infection biology that should help unravel pathogen infection strategies and the mechanisms by which host defense responses are overcome.
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Dss1 Is a 26S Proteasome Ubiquitin Receptor

Dss1 Is a 26S Proteasome Ubiquitin Receptor | Plant-microbe interaction | Scoop.it
Summary

The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome. The proteasome subunits Rpn10 and Rpn13 are known to bind ubiquitin, but genetic and biochemical data suggest the existence of at least one other substrate receptor. Here, we show that the phylogenetically conserved proteasome subunit Dss1 (Sem1) binds ubiquitin chains linked by K63 and K48. Atomic resolution data show that Dss1 is disordered and binds ubiquitin by binding sites characterized by acidic and hydrophobic residues. The complementary binding region in ubiquitin is composed of a hydrophobic patch formed by I13, I44, and L69 flanked by two basic regions. Mutations in the ubiquitin-binding site of Dss1 cause growth defects and accumulation of ubiquitylated proteins.

Via Christophe Jacquet
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Domain Dissection of AvrRxo1 for Suppressor, Avirulence and Cytotoxicity Functions

Domain Dissection of AvrRxo1 for Suppressor, Avirulence and Cytotoxicity Functions | Plant-microbe interaction | Scoop.it
AvrRxo1, a type III effector from Xanthomonas oryzae pv. oryzicola (Xoc) which causes bacterial leaf streak (BLS) in rice, can be recognised by non-host resistance protein Rxo1. It triggers a hypersensitive response (HR) in maize. Little is known regarding the virulence function of AvrRxo1. In this study, we determined that AvrRxo1 is able to suppress the HR caused by the non-host resistance recognition of Xanthomonas oryzae pv. oryzae (Xoo) by Nicotiana benthamiana. It is toxic, inducing cell death from transient expression in N. benthamiana, as well as in yeast. Among the four AvrRxo1 alleles from different Xoc strains, we concluded that the toxicity is abolished by a single amino acid substitution at residue 344 in two AvrRxo1 alleles. A series of truncations from the carboxyl terminus (C-terminus) indicate that the complete C-terminus of AvrRxo1 plays an essential role as a suppressor or cytotoxic protein. The C-terminus was also required for the avirulence function, but the last two residues were not necessary. The first 52 amino acids of N-terminus are unessential for toxicity. Point mutagenesis experiments indicate that the ATP/GTP binding site motif A is required for all three functions of AvrRxo1, and NLS is required for both the avirulence and the suppression of non-host resistance. The putative thiol protease site is only required for the cytotoxicity function. These results determine that AvrRxo1 plays a role in the complex interaction with host proteins after delivery into plant cells.
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36th New Phytologist Symposium: Cell biology at the plant–microbe interface, Munich, Germany 29 Nov – 1 Dec 2015

36th New Phytologist Symposium: Cell biology at the plant–microbe interface, Munich, Germany 29 Nov – 1 Dec 2015 | Plant-microbe interaction | Scoop.it

Symposium aim - We aim to organize a cutting edge meeting focused on the application of cell biology approaches to understand the mechanisms that diverse microbes use to manipulate plant cells to benefit their life styles. The meeting will bring together researchers working on a broad spectrum of microbes across different taxa (bacteria, fungi, oomycetes) that form a variety of different interactions (pathogenic, symbiotic) with plant organs/tissues (leaves, roots). With the explosion in microbial/host genome sequences and the identification of genes/proteins involved in these interactions, the focus of the field is moving rapidly towards using cell and molecular biology techniques and new imaging technologies to understand the molecular dialogue between plants and their microbial pathogens/symbionts. The need for a conference on this topic, the first of its type, is evidenced by the growing prominence of cell biology in the literature. Students and scientists in this field face many challenges in the application and interpretation of cell biology data and would greatly benefit from a specialized conference on this topic. The symposium will bring together a broad representation of researchers focussing on different cell biology aspects and will allow researchers across the different disciplines to present and exchange their recent advances in this important topic of plant biology.

Symposium rationale and scope - Plant organs are subject to colonisation and manipulation by microbes, and this requires reprogramming of host cell biology to accommodate microbial structures within tissues/cells and to mediate responses for proper immunity or for symbiosis. Host cell biology changes during microbial invasion were first reported more than 100 years ago based on microscopy studies revealing that many microbes project structures (haustoria, arbuscules) into plant cells that are enveloped with a specialized plant-­derived membrane and evidence now suggests an intimate molecular exchange takes place across these membrane interfaces. However, recent identification of some of the molecular players in these interactions is only now providing appropriate tools to analyse these events. The symposium will focus on advances in understanding the molecular interactions that occur between a microbe and its host at a cellular and subcellular level, such as:

how root and leaf cells accommodate microbial structures through biogenesis of specialized plant derived membranes, microbial invasion and spreading strategies (via stomata, roots, vasculature, plasmodesmata), the dynamic localization of cell surface and cytosolic receptors recognizing microbial signals the reprogramming of host membrane trafficking (focal accumulation, secretion), the delivery of microbial molecules from fungal and oomycete species into plant cells.

With recent advances in high resolution/throughput bioimaging we are gaining new insights into the cell biology mechanisms and pathways of plant cell interactions with diverse microbes. Therefore the symposium provides a timely and important opportunity to overview the application of these technologies to plant–microbe interactions, and to discuss recent discoveries emerging from diverse host–microbe interactions illustrating common underlying principles and differences of strategies used by the microbes to gain access to plant tissues/cells. The symposium will certainly trigger a wealth of discussions, exchange of findings and methodologies, and will promote new lines of research and ideas in this rapidly expanding field.


Via Kamoun Lab @ TSL, Nicolas Denancé
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Modulation of RNA Polymerase II Phosphorylation Downstream of Pathogen Perception Orchestrates Plant Immunity: Cell Host & Microbe

Modulation of RNA Polymerase II Phosphorylation Downstream of Pathogen Perception Orchestrates Plant Immunity: Cell Host & Microbe | Plant-microbe interaction | Scoop.it
Highlights


•RNA polymerase II CTD phosphatase (CPL3) mutants show enhanced immune gene activation
•MAMPs induce cyclin-dependent kinases CDKCs and RNA pol II CTD phosphorylation
•Direct CDKC phosphorylation by MAP kinase (MAPK) activates immune gene expression
•CPL3 counteracts MAPK-CDKC regulation via RNA pol II CTD dephosphorylation

 

Summary
Perception of microbe-associated molecular patterns (MAMPs) elicits host transcriptional reprogramming as part of the immune response. Although pathogen perception is well studied, the signaling networks orchestrating immune gene expression remain less clear. In a genetic screen for components involved in the early immune gene transcription reprogramming, we identified Arabidopsis RNA polymerase II C-terminal domain (CTD) phosphatase-like 3 (CPL3) as a negative regulator of immune gene expression. MAMP perception induced rapid and transient cyclin-dependent kinase C (CDKC)-mediated phosphorylation of Arabidopsis CTD. The CDKCs, which are in turn phosphorylated and activated by a canonical MAP kinase (MAPK) cascade, represent a point of signaling convergence downstream of multiple immune receptors. CPL3 directly dephosphorylated CTD to counteract MAPK-mediated CDKC regulation. Thus, modulation of the phosphorylation dynamics of eukaryotic RNA polymerase II transcription machinery by MAPKs, CTD kinases, and phosphatases constitutes an essential mechanism for rapid orchestration of host immune gene expression and defense upon pathogen attacks.

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GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell death in Arabidopsis

GRIM REAPER peptide binds to receptor kinase PRK5 to trigger cell death in Arabidopsis | Plant-microbe interaction | Scoop.it
Recognition of extracellular peptides by plasma membrane‐localized receptor proteins is commonly used in signal transduction. In plants, very little is known about how extracellular peptides are processed and activated in order to allow recognition by receptors. Here, we show that induction of cell death in planta by a secreted plant protein GRIM REAPER (GRI) is dependent on the activity of the type II metacaspase METACASPASE‐9. GRI is cleaved by METACASPASE‐9 in vitro resulting in the release of an 11 amino acid peptide. This peptide bound in vivo to the extracellular domain of the plasma membrane‐localized, atypical leucine‐rich repeat receptor‐like kinase POLLEN‐SPECIFIC RECEPTOR‐LIKE KINASE 5 (PRK5) and was sufficient to induce oxidative stress/ROS‐dependent cell death. This shows a signaling pathway in plants from processing and activation of an extracellular protein to recognition by its receptor.
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Curr Opin Microbiology: Targeting of plant pattern recognition receptor-triggered immunity by bacterial type-III secretion system effectors (2014)

Curr Opin Microbiology: Targeting of plant pattern recognition receptor-triggered immunity by bacterial type-III secretion system effectors (2014) | Plant-microbe interaction | Scoop.it

• Type-III effectors (T3Es) suppress plant immunity using multiple strategies.
• PRR-triggered immunity is redundantly targeted by multiple T3Es from a single bacterial strain.
• A single T3E can have multiple plant targets.
• A given immune component can be targeted by multiple T3Es.
• The study of T3Es reveals important immune components and unique biochemical processes.

 

During infection, microbes are detected by surface-localized pattern recognition receptors (PRRs), leading to an innate immune response that prevents microbial ingress. Therefore, successful pathogens must evade or inhibit PRR-triggered immunity to cause disease. In the past decade, a number of type-III secretion system effector (T3Es) proteins from plant pathogenic bacteria have been shown to suppress this layer of innate immunity. More recently, the detailed mechanisms of action have been defined for several of these effectors. Interestingly, effectors display a wide array of virulence targets, being able to prevent activation of immune receptors and to hijack immune signaling pathways. Besides being a fascinating example of pathogen-host co-evolution, effectors have also emerged as valuable tools to dissect important biological processes in host cells.


Via Kamoun Lab @ TSL
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The Calcium-Dependent Protein Kinase CPK28 Buffers Plant Immunity and Regulates BIK1 Turnover: Cell Host & Microbe

The Calcium-Dependent Protein Kinase CPK28 Buffers Plant Immunity and Regulates BIK1 Turnover: Cell Host & Microbe | Plant-microbe interaction | Scoop.it
Plant perception of pathogen-associated molecular patterns (PAMPs) triggers a phosphorylation relay leading to PAMP-triggered immunity (PTI). Despite increasing knowledge of PTI signaling, how immune homeostasis is maintained remains largely unknown. Here we describe a forward-genetic screen to identify loci involved in PTI and characterize the Arabidopsis calcium-dependent protein kinase CPK28 as a negative regulator of immune signaling. Genetic analyses demonstrate that CPK28 attenuates PAMP-triggered immune responses and antibacterial immunity. CPK28 interacts with and phosphorylates the plasma-membrane-associated cytoplasmic kinase BIK1, an important convergent substrate of multiple pattern recognition receptor (PRR) complexes. We find that BIK1 is rate limiting in PTI signaling and that it is continuously turned over to maintain cellular homeostasis. We further show that CPK28 contributes to BIK1 turnover. Our results suggest a negative regulatory mechanism that continually buffers immune signaling by controlling the turnover of this key signaling kinase.
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Functional analysis of plant defense suppression and activation by the Xanthomonas core type III effector XopX

Functional analysis of plant defense suppression and activation by the Xanthomonas core type III effector XopX | Plant-microbe interaction | Scoop.it
Many phytopathogenic type III secretion effectors (T3Es) have been shown to target and suppress plant immune signaling, but perturbation of the plant immune system by T3Es can also elicit a plant response. XopX is a “core” Xanthomonas T3E that contributes to growth and symptom development during Xanthomonas euvesicatoria (Xe) infection of tomato, but its functional role is undefined. We tested the effect of XopX on several aspects of plant immune signaling. XopX promoted ethylene production and plant cell death (PCD) during Xe infection of susceptible tomato and in transient expression assays in Nicotiana benthamiana, which is consistent with its requirement for the development of Xe-induced disease symptoms. Additionally, although XopX suppressed flagellin-induced reactive oxygen species, it promoted the accumulation of pattern-triggered immunity (PTI) gene transcripts. Surprisingly, XopX co-expression with other PCD elicitors resulted in delayed PCD, suggesting antagonism between XopX-dependent PCD and other PCD pathways. However, we found no evidence that XopX contributed to the suppression of effector-triggered immunity during Xe-tomato interactions, suggesting that XopX’s primary virulence role is to modulate PTI. These results highlight the dual role of a core Xanthomonas T3E in simultaneously suppressing and activating plant defense responses.
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Frontiers | The Salmonella effector protein SpvC, a phosphothreonine lyase is functional in plant cells | Plant-Microbe Interaction

Frontiers | The Salmonella effector protein SpvC, a phosphothreonine lyase is functional in plant cells | Plant-Microbe Interaction | Plant-microbe interaction | Scoop.it
Salmonella is one of the most prominent causes of food poisoning and growing evidence indicates that contaminated fruits and vegetables are an increasing concern for human health. Successful infection demands the suppression of the host immune system, which is often achieved via injection of bacterial effector proteins into host cells. In this report we present the function of Salmonella effector protein in plant cell, supporting the new concept of trans-kingdom competence of this bacterium. We screened a range of Salmonella Typhimurium effector proteins for interference with plant immunity. Among these, the phosphothreonine lyase SpvC attenuated the induction of immunity-related genes when present in plant cells. Using in vitro and in vivo systems we show that this effector protein interacts with and dephosphorylates activated Arabidopsis Mitogen-activated Protein Kinase 6 (MPK6), thereby inhibiting defense signaling. Moreover, the requirement of Salmonella SpvC was shown by the decreased proliferation of the ΔspvC mutant in Arabidopsis plants. These results suggest that some Salmonella effector proteins could have a conserved function during proliferation in different hosts. The fact that Salmonella and other Enterobacteriaceae use plants as hosts strongly suggests that plants represent a much larger reservoir for animal pathogens than so far estimated.
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Perturbation of host ubiquitin systems by plant pathogen/pest effector proteins - Banfield - Cellular Microbiology - Wiley Online Library

Perturbation of host ubiquitin systems by plant pathogen/pest effector proteins - Banfield - Cellular Microbiology - Wiley Online Library | Plant-microbe interaction | Scoop.it
Microbial pathogens and pests of animals and plants secrete effector proteins into host cells, altering cellular physiology to the benefit of the invading parasite. Research in the past decade has delivered significant new insights into the molecular mechanisms of how these effector proteins function, with a particular focus on modulation of host immunity-related pathways. One host system that has emerged as a common target of effectors is the ubiquitination system in which substrate proteins are post-translationally modified by covalent conjugation with the small protein ubiquitin. This modification, typically via isopeptide bond formation through a lysine side-chain of ubiquitin, can result in target degradation, re-localisation, altered activity or affect protein-protein interactions. In this review I focus primarily on how effector proteins from bacterial and filamentous pathogens of plants and pests perturb host ubiquitination pathways that ultimately include the 26S proteasome. The activities of these effectors, in how they affect ubiquitin pathways in plants, reveals how pathogens have evolved to identify and exploit weaknesses in this system that deliver increased pathogen fitness.
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Genome Biology | Abstract | Transcriptomic analysis reveals tomato genes whose expression is induced specifically during effector-triggered immunity and identifies the Epk1 protein kinase which is ...

Genome Biology | Abstract | Transcriptomic analysis reveals tomato genes whose expression is induced specifically during effector-triggered immunity and identifies the Epk1 protein kinase which is ... | Plant-microbe interaction | Scoop.it

Background: Plants have two related immune systems to defend themselves against pathogen attack. Initially, pattern-triggered immunity is activated upon recognition of microbe-associated molecular patterns by pattern recognition receptors. Pathogenic bacteria deliver effector proteins into the plant cell that interfere with this immune response and promote disease. However, some plants express resistance proteins that detect the presence of specific effectors leading to a robust defense response referred to as effector-triggered immunity. The interaction of tomato with Pseudomonas syringae pv. tomato is an established model system for understanding the molecular basis of these plant immune responses.ResultsWe apply high-throughput RNA sequencing to this pathosystem to identify genes whose expression changes specifically during pattern-triggered or effector-triggered immunity. We then develop reporter genes for each of these responses that will enable characterization of the host response to the large collection of P. s. pv. tomato strains that express different combinations of effectors. Virus-induced gene silencing of 30 of the effector-triggered immunity-specific genes identifies Epk1 which encodes a predicted protein kinase from a family previously unknown to be involved in immunity. Knocked-down expression of Epk1 compromises effector-triggered immunity triggered by three bacterial effectors but not by effectors from non-bacterial pathogens. Epistasis experiments indicate that Epk1 acts upstream of effector-triggered immunity-associated MAP kinase signaling.ConclusionsUsing RNA-seq technology we identify genes involved in specific immune responses. A functional genomics screen led to the discovery of Epk1, a novel predicted protein kinase required for plant defense activation upon recognition of three different bacterial effectors.

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Myosins VIII and XI Play Distinct Roles in Reproduction and Transport of Tobacco Mosaic Virus

Myosins VIII and XI Play Distinct Roles in Reproduction and Transport of Tobacco Mosaic Virus | Plant-microbe interaction | Scoop.it
Viruses are obligatory parasites that depend on host cellular factors for their replication as well as for their local and systemic movement to establish infection. Although myosin motors are thought to contribute to plant virus infection, their exact roles in the specific infection steps have not been addressed. Here we investigated the replication, cell-to-cell and systemic spread of Tobacco mosaic virus (TMV) using dominant negative inhibition of myosin activity. We found that interference with the functions of three class VIII myosins and two class XI myosins significantly reduced the local and long-distance transport of the virus. We further determined that the inactivation of myosins XI-2 and XI-K affected the structure and dynamic behavior of the ER leading to aggregation of the viral movement protein (MP) and to a delay in the MP accumulation in plasmodesmata (PD). The inactivation of myosin XI-2 but not of myosin XI-K affected the localization pattern of the 126k replicase subunit and the level of TMV accumulation. The inhibition of myosins VIII-1, VIII-2 and VIII-B abolished MP localization to PD and caused its retention at the plasma membrane. These results suggest that class XI myosins contribute to the viral propagation and intracellular trafficking, whereas myosins VIII are specifically required for the MP targeting to and virus movement through the PD. Thus, TMV appears to recruit distinct myosins for different steps in the cell-to-cell spread of the infection.
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Nucleotide-binding oligomerization domain-like receptor cooperativity in effector-triggered immunity

Nucleotide-binding oligomerization domain-like receptor cooperativity in effector-triggered immunity | Plant-microbe interaction | Scoop.it

Intracellular nucleotide-binding oligomerization domain (NOD)-like receptors (NLRs) are basic elements of innate immunity in plants and animals. Whereas animal NLRs react to conserved microbe- or damage-associated molecular patterns, plant NLRs intercept the actions of diverse pathogen virulence factors (effectors). In this review, we discuss recent genetic and molecular evidence for functional NLR pairs, and discuss the significance of NLR self-association and heteromeric NLR assemblies in the triggering of downstream signaling pathways. We highlight the versatility and impact of cooperating NLR pairs that combine pathogen sensing with the initiation of defense signaling in both plant and animal immunity. We propose that different NLR receptor molecular configurations provide opportunities for fine-tuning resistance pathways and enhancing the host's pathogen recognition spectrum to keep pace with rapidly evolving microbial populations.

  
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