scholarly journals AtSERPIN1 is an inhibitor of the metacaspase AtMC1-mediated cell death and autocatalytic processing in planta

2017 ◽  
Vol 218 (3) ◽  
pp. 1156-1166 ◽  
Author(s):  
Saul Lema Asqui ◽  
Dominique Vercammen ◽  
Irene Serrano ◽  
Marc Valls ◽  
Susana Rivas ◽  
...  
Keyword(s):  
Cell Death ◽  
In Planta ◽  
Autocatalytic Processing

scholarly journals Autocatalytic Processing of HtrA2/Omi Is Essential for Induction of Caspase-dependent Cell Death through Antagonizing XIAP

2004 ◽  
Vol 279 (36) ◽  
pp. 37588-37596 ◽  
Author(s):  
Young-Mo Seong ◽  
Ju-Youn Choi ◽  
Hyo-Jin Park ◽  
Ki-Joong Kim ◽  
Sang-Gun Ahn ◽  
...  
Keyword(s):  
Cell Death ◽  
Autocatalytic Processing ◽  
Dependent Cell

scholarly journals Xanthomonas Filamentous Hemagglutinin-Like Protein Fha1 Interacts with Pepper Hypersensitive-Induced Reaction Protein CaHIR1 and Functions as a Virulence Factor in Host Plants

2013 ◽  
Vol 26 (12) ◽  
pp. 1441-1454 ◽  
Author(s):  
Hyong Woo Choi ◽  
Dae Sung Kim ◽  
Nak Hyun Kim ◽  
Ho Won Jung ◽  
Jong Hyun Ham ◽  
...  
Keyword(s):  
Cell Death ◽  
Virulence Factor ◽  
Xanthomonas Campestris ◽  
Host Plants ◽  
Bimolecular Fluorescence Complementation ◽  
In Planta ◽  
Pr Genes ◽  
Filamentous Hemagglutinin ◽  
Cell Death Response ◽  
Induced Reaction

Pathogens have evolved a variety of virulence factors to infect host plants successfully. We previously identified the pepper plasma-membrane-resident hypersensitive-induced reaction protein (CaHIR1) as a regulator of plant disease- and immunity-associated cell death. Here, we identified the small filamentous hemagglutinin-like protein (Fha1) of Xanthomonas campestris pv. vesicatoria as an interacting partner of CaHIR1 using yeast two-hybrid screening. Coimmunoprecipitation and bimolecular fluorescence complementation experiments revealed that Fha1 specifically interacts with CaHIR1 in planta. The endocytic tracker FM4-64 staining showed that the CaHIR1-Fha1 complex localizes in the endocytic vesicle-like structure. The X. campestris pv. vesicatoria Δfha1 mutant strain exhibited significantly increased surface adherence but reduced swarming motility. Mutation of fha1 inhibited the growth of X. campestris pv. vesicatoria and X. campestris pv. vesicatoria ΔavrBsT in tomato and pepper leaves, respectively, suggesting that Fha1 acts as a virulence factor in host plants. Transient expression of fha1 and also infiltration with purified Fha1 proteins induced disease-associated cell death response through the interaction with CaHIR1 and suppressed the expression of pathogenesis-related (PR) genes. Silencing of CaHIR1 in pepper significantly reduced ΔavrBsT growth and Fha1-triggered susceptibility cell death. Overexpression of fha1 in Arabidopsis retarded plant growth and triggered disease-associated cell death, resulting in altered disease susceptibility. Taken together, these results suggest that the X. campestris pv. vesicatoria virulence factor Fha1 interacts with CaHIR1, induces susceptibility cell death, and suppresses PR gene expression in host plants.

scholarly journals Use of a Secretion Trap Screen in Pepper Following Phytophthora capsici Infection Reveals Novel Functions of Secreted Plant Proteins in Modulating Cell Death

2011 ◽  
Vol 24 (6) ◽  
pp. 671-684 ◽  
Author(s):  
Seon-In Yeom ◽  
Hyang-Ku Baek ◽  
Sang-Keun Oh ◽  
Won-Hee Kang ◽  
Sang Jik Lee ◽  
...  
Keyword(s):  
Cell Death ◽  
Capsicum Annuum ◽  
Pseudomonas Syringae ◽  
Signal Sequence ◽  
Phytophthora Capsici ◽  
Tobacco Rattle Virus ◽  
Secreted Proteins ◽  
In Planta ◽  
Cell Wall Modification ◽  
Cas Genes

In plants, the primary defense against pathogens is mostly inducible and associated with cell wall modification and defense-related gene expression, including many secreted proteins. To study the role of secreted proteins, a yeast-based signal-sequence trap screening was conducted with the RNA from Phytophthora capsici-inoculated root of Capsicum annuum ‘Criollo de Morelos 334’ (CM334). In total, 101 Capsicum annuum secretome (CaS) clones were isolated and identified, of which 92 were predicted to have a secretory signal sequence at their N-terminus. To identify differences in expressed CaS genes between resistant and susceptible cultivars of pepper, reverse Northern blots and real-time reverse-transcription polymerase chain reaction were performed with RNA samples isolated at different time points following P. capsici inoculation. In an attempt to assign biological functions to CaS genes, we performed in planta knock-down assays using the Tobacco rattle virus-based gene-silencing method. Silencing of eight CaS genes in pepper resulted in suppression of the cell death induced by the non-host bacterial pathogen (Pseudomonas syringae pv. tomato T1). Three CaS genes induced phenotypic abnormalities in silenced plants and one, CaS259 (PR4-l), caused both cell death suppression and perturbed phenotypes. These results provide evidence that the CaS genes may play important roles in pathogen defense as well as developmental processes.

scholarly journals HSP70s Enhance a Phytophthora infestans Effector-Induced Cell Death via an MAPK Cascade in Nicotiana benthamiana

2018 ◽  
Vol 31 (3) ◽  
pp. 356-362 ◽  
Author(s):  
Joo Hyun Lee ◽  
So Eui Lee ◽  
Soohyun Oh ◽  
Eunyoung Seo ◽  
Doil Choi
Keyword(s):  
Cell Death ◽  
Phytophthora Infestans ◽  
Mode Of Action ◽  
Nicotiana Benthamiana ◽  
Host Plants ◽  
Mitogen Activated Protein Kinase ◽  
Defense System ◽  
In Planta ◽  
Pathogen Effectors ◽  
Mitogen Activated Protein

A destructive pathogen, Phytophthora infestans, secretes hundreds of effectors for successful survival in its host plants. The effectors modulate the plant defense system at diverse cellular compartments to take an advantage of pathogen survivals. A few research studies have shown the mode of action of each effector and their interacting proteins in plant cells. Here, we investigated the mode of action of a P. infestans effector, Pi23226, which induces cell death in Nicotiana benthamiana. To identify its host factors, we performed coimmunoprecipitation and liquid chromatography-mass spectrometry, and selected members of heat shock protein 70 (HSP70s) as candidates. These HSP70s, known to function as chaperones, were associated with Pi23226 in planta and accelerated Pi23226-induced cell death. Additionally, they were found to be involved in plant basal defense by suppressing the growth of P. infestans. We also found that specific components of a mitogen-activated protein kinase cascade were involved in Pi23226-induced cell death. Our findings show that HSP70s functions in defense systems by regulating effector-triggered cell death and by suppressing the growth of the pathogen. This suggests that host plants manipulate the ubiquitous proteins to detect pathogen effectors for functioning in the defense system.

scholarly journals The ELR-SOBIR1 Complex Functions as a Two-Component Receptor-Like Kinase to Mount Defense Against Phytophthora infestans

2018 ◽  
Vol 31 (8) ◽  
pp. 795-802 ◽  
Author(s):  
Emmanouil Domazakis ◽  
Doret Wouters ◽  
Richard G. F. Visser ◽  
Sophien Kamoun ◽  
Matthieu H. A. J. Joosten ◽  
...  
Keyword(s):  
Cell Death ◽  
Phytophthora Infestans ◽  
Defense Responses ◽  
Virus Induced Gene Silencing ◽  
In Planta ◽  
Basal Resistance ◽  
Downstream Signaling ◽  
Receptor Like Kinase ◽  
Signaling Domain ◽  
Signaling Activation

The ELICITIN RESPONSE protein (ELR) from Solanum microdontum can recognize INF1 elicitin of Phytophthora infestans and trigger defense responses. ELR is a receptor-like protein (RLP) that lacks a cytoplasmic signaling domain and is anticipated to require interaction with a signaling-competent receptor-like kinase. SUPPRESSOR OF BIR1-1 (SOBIR1) has been proposed as a general interactor for RLPs involved in immunity and, as such, is a potential interactor for ELR. Here, we investigate whether SOBIR1 is required for response to INF1 and resistance to P. infestans and whether it associates with ELR. Our results show that virus-induced gene silencing of SOBIR1 in Nicotiana benthamiana leads to loss of INF1-triggered cell death and increased susceptibility to P. infestans. Using genetic complementation, we found that the kinase activity of SOBIR1 is required for INF1-triggered cell death. Coimmunoprecipitation experiments showed that ELR constitutively associates with potato SOBIR1 in planta, forming a bipartite receptor complex. Upon INF1 elicitation, this ELR-SOBIR1 complex recruits SERK3 (SOMATIC EMBRYOGENESIS RECEPTOR KINASE 3) leading to downstream signaling activation. Overall, our study shows that SOBIR1 is required for basal resistance to P. infestans and for INF1-triggered cell death and functions as an adaptor kinase for ELR.

scholarly journals Arabidopsis Lectin Receptor Kinases LecRK-IX.1 and LecRK-IX.2 Are Functional Analogs in Regulating Phytophthora Resistance and Plant Cell Death

2015 ◽  
Vol 28 (9) ◽  
pp. 1032-1048 ◽  
Author(s):  
Yan Wang ◽  
Jan H. G. Cordewener ◽  
Antoine H. P. America ◽  
Weixing Shan ◽  
Klaas Bouwmeester ◽  
...  
Keyword(s):  
Cell Death ◽  
Abc Transporter ◽  
Mitogen Activated Protein Kinase ◽  
Mass Spectrometry Analysis ◽  
In Planta ◽  
Lectin Domain ◽  
Spectrometry Analysis ◽  
Lectin Receptor ◽  
Receptor Kinases ◽  
Phytophthora Resistance

L-type lectin receptor kinases (LecRK) are potential immune receptors. Here, we characterized two closely-related Arabidopsis LecRK, LecRK-IX.1 and LecRK-IX.2, of which T-DNA insertion mutants showed compromised resistance to Phytophthora brassicae and Phytophthora capsici, with double mutants showing additive susceptibility. Overexpression of LecRK-IX.1 or LecRK-IX.2 in Arabidopsis and transient expression in Nicotiana benthamiana increased Phytophthora resistance but also induced cell death. Phytophthora resistance required both the lectin domain and kinase activity, but for cell death, the lectin domain was not needed. Silencing of the two closely related mitogen-activated protein kinase genes NbSIPK and NbNTF4 in N. benthamiana completely abolished LecRK-IX.1-induced cell death but not Phytophthora resistance. Liquid chromatography-mass spectrometry analysis of protein complexes coimmunoprecipitated in planta with LecRK-IX.1 or LecRK-IX.2 as bait, resulted in the identification of the N. benthamiana ABC transporter NbPDR1 as a potential interactor of both LecRK. The closest homolog of NbPDR1 in Arabidopsis is ABCG40, and coimmunoprecipitation experiments showed that ABCG40 associates with LecRK-IX.1 and LecRK-IX.2 in planta. Similar to the LecRK mutants, ABCG40 mutants showed compromised Phytophthora resistance. This study shows that LecRK-IX.1 and LecRK-IX.2 are Phytophthora resistance components that function independent of each other and independent of the cell-death phenotype. They both interact with the same ABC transporter, suggesting that they exploit similar signal transduction pathways.

scholarly journals The necrotrophic effector ToxA from Parastagonospora nodorum interacts with wheat NHL proteins to facilitate Tsn1-mediated necrosis

2021 ◽  
Author(s):  
Bayantes Dagvadorj ◽  
Megan A. Outram ◽  
Simon J. Williams ◽  
Peter S. Solomon
Keyword(s):  
Cell Death ◽  
Confocal Microscopy ◽  
Molecular Mechanisms ◽  
Wheat Cultivars ◽  
In Planta ◽  
Yeast Two Hybrid ◽  
Induce Cell Death ◽  
Parastagonospora Nodorum ◽  
Necrotrophic Effector ◽  
Two Hybrid

SummaryThe plant pathogen Parastagonospora nodorum secretes necrotrophic effectors to promote disease. These effectors induce cell death on wheat cultivars carrying dominant susceptibility genes in an inverse gene-for-gene manner. However, the molecular mechanisms underpinning these interactions and resulting cell death remain unclear. Here, we used a yeast-two-hybrid library approach to identify wheat proteins that interact with the necrotrophic effector ToxA. Using this strategy, we identified an interaction between ToxA and a wheat transmembrane NDR/HIN1-like protein (TaNHL10) and confirmed the interaction using in-planta co-immunoprecipitation and confocal microscopy co-localization analysis. We showed that the C-terminus of TaNHL10 is extracellular whilst the N-terminus was localized in the cytoplasm. Further analyses using yeast-two-hybrid and confocal microscopy co-localization showed that ToxA interacts with the C-terminal LEA2 extracellular domain of TaNHL10. Random mutagenesis was then used to identify a ToxA mutant, ToxAN109D, which was unable to interact with TaNHL10 in yeast-two-hybrid assays. Subsequent heterologous expression and purification of ToxAN109D in Nicotiania benthamiana revealed that the mutated protein was unable to induce necrosis on Tsn1-dominant wheat cultivars confirming that the interaction of ToxA with TaNHL10 is required to induce cell death. Collectively, these data advance our understanding on how ToxA induces cell death during infection and further highlights the importance of host cell surface interactions in necrotrophic pathosystems.

scholarly journals The flavin monooxygenase Bs3 triggers cell death in plants, impairs growth in yeast and produces H2O2in vitro

2021 ◽  
Author(s):  
Christina Krönauer ◽  
Thomas Lahaye
Keyword(s):  
Cell Death ◽  
Nadph Oxidase ◽  
Transcriptional Activation ◽  
Oxidase Activity ◽  
Bacterial Pathogen ◽  
Histochemical Staining ◽  
In Planta ◽  
Transcription Activator ◽  
Nadph Oxidase Activity

ABSTRACTThe pepper resistance gene Bs3 triggers a hypersensitive response (HR) upon transcriptional activation by the corresponding transcription activator-like effector AvrBs3 from the bacterial pathogen Xanthomonas. Bs3 is homologous to flavin monooxygenases (FMOs), an enzyme class that has NADPH oxidase activity and can produce H2O2, a hallmark metabolite in plant immune reactions. Histochemical staining of infected pepper leaves and a translational fusion of Bs3 to the redox reporter roGFP2 both indicated that the Bs3-dependent HR induces a local increase in H2O2 levels in planta. Moreover, our in vitro studies with recombinant Bs3 protein confirmed its NADPH oxidase activity. To test if the NADPH oxidation of Bs3 induces HR, we adapted previous studies which have uncovered mutations in fungal FMOs that result in higher NADPH oxidase activity. We replicated one of these mutations and demonstrated that the generated recombinant Bs3S211A protein has twofold higher NADPH oxidase activity than wildtype Bs3 in vitro. Translational fusions to roGFP2 showed that Bs3S211A also had increased NADPH oxidase activity in planta. Interestingly, while the mutant derivative Bs3S211A had an increase in NADPH oxidase capacity, it did not trigger HR in planta. Ultimately, this reveals that Bs3 produces H2O2in planta, but that the H2O2 produced by Bs3 on its own is not sufficient to trigger HR. We also demonstrated that expression of Bs3 not only triggered HR in plants, but also inhibited proliferation of yeast, which lends this model system to be utilized for the genetic dissection of Bs3 function in future studies.One sentence summaryThe executor-type resistance protein Bs3 from pepper (Capsicum annuum) acts as an NADPH oxidase but reactive oxygen species produced by Bs3 are not sufficient to trigger plant cell death

scholarly journals DspA/E, a Type III Effector Essential for Erwinia amylovora Pathogenicity and Growth In Planta, Induces Cell Death in Host Apple and Nonhost Tobacco Plants

2006 ◽  
Vol 19 (1) ◽  
pp. 16-24 ◽  
Author(s):  
Tristan Boureau ◽  
Hayat ElMaarouf-Bouteau ◽  
Amélie Garnier ◽  
Marie-Noëlle Brisset ◽  
Claude Perino ◽  
...  
Keyword(s):  
Cell Death ◽  
Type Iii Secretion ◽  
Erwinia Amylovora ◽  
Marker Gene ◽  
Defense Responses ◽  
In Planta ◽  
Callose Deposition ◽  
Type Iii Effector ◽  
Type Iii

Erwinia amylovora is responsible for fire blight, a necrotic disease of apples and pears. E. amylovora relies on a type III secretion system (TTSS) to induce disease on hosts and hypersensitive response (HR) on nonhost plants. The DspA/E protein is essential for E. amylovora pathogenicity and is secreted via the TTSS in vitro. DspA/E belongs to a type III effector family that is conserved in several phytopathogenic bacteria. In E. amylovora, DspA/E has been implicated in the generation of an oxidative stress during disease and the suppression of callose deposition. We investigated the fate of DspA/E in planta. DspA/E delivered artificially to apple or tobacco cells by agroinfection induced necrotic symptoms, indicating that DspA/E was probably injected via the TTSS. We confirmed that DspA/E acts as a major cell-death inducer during disease and HR, because the dspA/E mutant is severely impaired in its ability to induce electrolyte leakage in apple and tobacco leaves. Expression of the defense marker gene PR1 was delayed when dspA/E was transiently expressed in tobacco, suggesting that DspA/E-mediated necrosis may be associated with an alteration of defense responses.

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