The cyclic lipopeptide orfamide induces systemic resistance in rice to Cochliobolus miyabeanus but not to Magnaporthe oryzae

2017 ◽  
Vol 36 (11) ◽  
pp. 1731-1746 ◽  
Author(s):  
Zongwang Ma ◽  
Marc Ongena ◽  
Monica Höfte
Keyword(s):  
Magnaporthe Oryzae ◽  
Systemic Resistance ◽  
Cyclic Lipopeptide ◽  
Cochliobolus Miyabeanus

Activation of Systemic Resistance to Magnaporthe oryzae in Rice by Substances Produced by Fusarium solani Isolated from Soil

2014 ◽  
Vol 162 (7-8) ◽  
pp. 434-441 ◽  
Author(s):  
Lih-Ling Chern ◽  
Hsiu-Chuan Lin ◽  
Chieh-Ting Chang ◽  
Wen-Hsiung Ko
Keyword(s):  
Magnaporthe Oryzae ◽  
Fusarium Solani ◽  
Systemic Resistance

scholarly journals Cyclic Lipopeptide Surfactant Production by Pseudomonas fluorescens SS101 Is Not Required for Suppression of Complex Pythium spp. Populations

2007 ◽  
Vol 97 (10) ◽  
pp. 1348-1355 ◽  
Author(s):  
M. Mazzola ◽  
X. Zhao ◽  
M. F. Cohen ◽  
J. M. Raaijmakers
Keyword(s):  
Pseudomonas Fluorescens ◽  
Significant Role ◽  
Disease Suppression ◽  
Systemic Resistance ◽  
Root Infection ◽  
Apple Rootstocks ◽  
Wheat Seedlings ◽  
Cyclic Lipopeptide ◽  
Plant Assays

Previously, the zoosporicidal activity and control of Pythium root rot of flower bulbs by Pseudomonas fluorescens SS101 was attributed, in part, to the production of the cyclic lipopeptide surfactant massetolide A. The capacity of strain SS101 and its surfactant-deficient massA mutant 10.24 to suppress populations and root infection by complex Pythium spp. communities resident in orchard soils was assessed on apple and wheat seedlings and on apple rootstocks. Both strains initially became established in soil and persisted in the rhizosphere at similar population densities; however, massA mutant 10.24 typically was detected at higher populations in the wheat rhizosphere and soil at the end of each experiment. Both strains effectively suppressed resident Pythium populations to an equivalent level in the presence or absence of plant roots, and ultimately suppressed Pythium root infection to the same degree on all host plants. When split-root plant assays were employed, neither strain suppressed Pythium spp. infection of the component of the root system physically separated from the bacterium, suggesting that induced systemic resistance did not play a role in Pythium control. Strain SS101 only marginally suppressed in vitro growth of Pythium spp. and growth was not inhibited in the presence of mutant 10.24. When incorporated into the growth medium, the cyclic lipopeptide massetolide A significantly slowed the rate of hyphal expansion for all Pythium spp. examined. Differences in sensitivity were observed among species, with Pythium heterothallicum, P. rostratum, and P. ultimum var. ultimum exhibiting significantly greater tolerance. Pythium spp. populations indigenous to the two soils employed were composed primarily of P. irregulare, P. sylvaticum, and P. ultimum var. ultimum. These Pythium spp. either do not or rarely produce zoospores, which could account for the observation that both SS101 and mutant 10.24 were equally effective in disease control. Collectively, the results showed that (i) Pseudomonas fluorescens SS101 is very effective in controlling diverse Pythium populations on different crops grown in different soils and (ii) production of the cyclic lipopeptide massetolide A does not play a significant role in disease suppression. Other, as yet undefined mechanisms appear to play a significant role in the interaction between P. fluorescens SS101 and soilborne Pythium spp. communities.

scholarly journals Bacillus cabrialesii BH5 Protects Tomato Plants Against Botrytis cinerea by Production of Specific Antifungal Compounds

2021 ◽  
Vol 12 ◽  
Author(s):  
Lu Zhou ◽  
Chunxu Song ◽  
Claudia Y. Muñoz ◽  
Oscar P. Kuipers
Keyword(s):  
Botrytis Cinerea ◽  
High Performance ◽  
Gray Mold ◽  
Plant Diseases ◽  
Systemic Resistance ◽  
Transcription Analysis ◽  
Tomato Plants ◽  
Global Food Security ◽  
Cyclic Lipopeptide

The gray mold caused by the phytopathogen Botrytis cinerea presents a threat to global food security. For the biological regulation of several plant diseases, Bacillus species have been extensively studied. In this work, we explore the ability of a bacterial strain, Bacillus cabrialesii BH5, that was isolated from tomato rhizosphere soil, to control the fungal pathogen B. cinerea. Strain B. cabrialesii BH5 showed a strong antifungal activity against B. cinerea. A compound was isolated and identified as a cyclic lipopeptide of the fengycin family by high-performance liquid chromatography and tandem mass spectrometry (ESI-MS/MS) that we named fengycin H. The fengycin H-treated hyphae of B. cinerea displayed stronger red fluorescence than the control, which is clearly indicating that fengycin H triggered the hyphal cell membrane defects. Moreover, root inoculation of tomato seedlings with BH5 effectively promoted the growth of tomato plants. Transcription analysis revealed that both BH5 and fengycin H stimulate induced systemic resistance of tomato plants via the jasmonic acid signaling pathway and provide a strong biocontrol effect in vivo. Therefore, the strain BH5 and fengycin H are very promising candidates for biological control of B. cinerea and the associated gray mold.

scholarly journals Cellular Responses of the Late Blight Pathogen Phytophthora infestans to Cyclic Lipopeptide Surfactants and Their Dependence on G Proteins

2009 ◽  
Vol 75 (15) ◽  
pp. 4950-4957 ◽  
Author(s):  
Judith E. van de Mortel ◽  
Ha Tran ◽  
Francine Govers ◽  
Jos M. Raaijmakers
Keyword(s):  
Late Blight ◽  
Phytophthora Infestans ◽  
G Protein ◽  
G Proteins ◽  
Developmental Stages ◽  
Cellular Responses ◽  
Systemic Resistance ◽  
Loss Of Function ◽  
Α Subunit ◽  
Cyclic Lipopeptide

ABSTRACT Oomycete pathogens cause major yield losses for many crop plants, and their control depends heavily on agrochemicals. Cyclic lipopeptides (CLPs) were recently discovered as a new class of natural compounds with strong activities against oomycetes. The CLP massetolide A (Mass A), produced by Pseudomonas fluorescens, has zoosporicidal activity, induces systemic resistance, and reduces late blight in tomato. To gain further insight into the modes of action of CLPs, the effects of Mass A on pore formation, mycelial growth, sporangium formation, and zoospore behavior were investigated, as was the involvement of G proteins in the sensitivity of Phytophthora infestans to Mass A. The results showed that Mass A induced the formation of transmembrane pores with an estimated size of between 1.2 and 1.8 nm. Dose-response experiments revealed that zoospores were the most sensitive to Mass A, followed by mycelium and cysts. Mass A significantly reduced sporangium formation and caused increased branching and swelling of hyphae. At relatively low concentrations, Mass A induced encystment of zoospores. It had no effect on the chemotactic response of zoospores but did adversely affect zoospore autoaggregation. A loss-of-function transformant of P. infestans lacking the G-protein α subunit was more sensitive to Mass A, whereas a gain-of-function transformant required a higher Mass A concentration to interfere with zoospore aggregation. Results indicate that Mass A disturbs various developmental stages in the life cycle of P. infestans and suggest that the cellular responses of P. infestans to this CLP are, in part, dependent on G-protein signaling.

scholarly journals Induction of Systemic Resistant Molecules in Phylloplane of Rice Plants against Magnaporthe oryzae by Pseudomonas fluorescens

2020 ◽  
pp. 25-36
Author(s):  
S. Suguna ◽  
S. Parthasarathy ◽  
G. Karthikeyan
Keyword(s):  
Magnaporthe Oryzae ◽  
Biocontrol Agents ◽  
Blast Disease ◽  
Systemic Resistance ◽  
Defense Enzymes ◽  
Leaf Blast ◽  
Native Page ◽  
Challenge Inoculation ◽  
Rice Plants ◽  
Significant Disease

Rice blast caused by ascomycetes fungus Magnaporthe oryzae, is mostly considered the utmost significant disease of rice worldwide since its widespread dissemination and destructiveness under conducive conditions. Experiments were conducted in phylloplane of rice plants to study the induction of various defense enzymes and accumulation of phenol by three biocontrol agents viz., P. fluorescens talc (Pf1), liquid formulation with TNAU - Pf1 and Biocure - B under pot culture. The application of bioformulatons of P. flourescens triggered the activity of three defense related enzymes viz., peroxidase (PO), polyphenol oxidase (PPO) and phenylalanine ammonia lyase (PAL) and SOD were induced and the accumulation of phenol was also noticed in phylloplane rice plant upon challenge inoculation with Magnaporthe oryzae the causal agent for leaf blast disease in rice. The activities of defense enzymes reached a peak at three days after inoculation (DAI) with the pathogen. Native PAGE analysis revealed the expression of an additional isoforms of PO, PPO, SOD and catalase were observed in biocontrol agents treated seedlings due to induced systemic resistance (ISR) induction.

scholarly journals Induction of Salicylic Acid–Mediated Defense Response in Perennial Ryegrass Against Infection by Magnaporthe oryzae

2014 ◽  
Vol 104 (6) ◽  
pp. 614-623 ◽  
Author(s):  
Alamgir Rahman ◽  
Gretchen A. Kuldau ◽  
Wakar Uddin
Keyword(s):  
Salicylic Acid ◽  
Perennial Ryegrass ◽  
Magnaporthe Oryzae ◽  
Leaf Spot ◽  
Disease Incidence ◽  
Gray Leaf Spot ◽  
Systemic Resistance ◽  
Leaf Spot Disease ◽  
Callose Deposition ◽  
Expression Levels

Incorporation of plant defense activators is an innovative approach to development of an integrated strategy for the management of turfgrass diseases. The effects of salicylic acid (SA), benzothiadiazole (BTH, chemical analog of SA), jasmonic acid (JA), and ethephon (ET, an ethylene-releasing compound) on development of gray leaf spot in perennial ryegrass (Lolium perenne L.) caused by Magnaporthe oryzae were evaluated. Gray leaf spot disease incidence and severity were significantly decreased when plants were treated prior to inoculation with SA, BTH, and partially by ET but not by JA. Accumulation of endogenous SA and elevated expression of pathogenesis-related (PR)-1, PR-3.1, and PR-5 genes were associated with inoculation of plants by M. oryzae. Treatment of plants with SA enhanced expression levels of PR-3.1 and PR-5 but did not affect the PR-1 level, whereas BTH treatment enhanced relative expression levels of all three PR genes. Microscopic observations of leaves inoculated with M. oryzae revealed higher frequencies of callose deposition at the penetration sites in SA- and BTH-treated plants compared with the control plants (treated with water). These results suggest that early and higher induction of these genes by systemic resistance inducers may provide perennial ryegrass with a substantial advantage to defend against infection by M. oryzae.

Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1

2019 ◽  
Vol 476 (21) ◽  
pp. 3227-3240 ◽  
Author(s):  
Shanshan Wang ◽  
Yanxiang Zhao ◽  
Long Yi ◽  
Minghe Shen ◽  
Chao Wang ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Conformational Changes ◽  
Magnaporthe Oryzae ◽  
Structural Information ◽  
Complex Structure ◽  
Critical Role ◽  
Catalytic Process ◽  
Structural Basis ◽  
Salt Bridges ◽  
Terminal Domain

Trehalose-6-phosphate (T6P) synthase (Tps1) catalyzes the formation of T6P from UDP-glucose (UDPG) (or GDPG, etc.) and glucose-6-phosphate (G6P), and structural basis of this process has not been well studied. MoTps1 (Magnaporthe oryzae Tps1) plays a critical role in carbon and nitrogen metabolism, but its structural information is unknown. Here we present the crystal structures of MoTps1 apo, binary (with UDPG) and ternary (with UDPG/G6P or UDP/T6P) complexes. MoTps1 consists of two modified Rossmann-fold domains and a catalytic center in-between. Unlike Escherichia coli OtsA (EcOtsA, the Tps1 of E. coli), MoTps1 exists as a mixture of monomer, dimer, and oligomer in solution. Inter-chain salt bridges, which are not fully conserved in EcOtsA, play primary roles in MoTps1 oligomerization. Binding of UDPG by MoTps1 C-terminal domain modifies the substrate pocket of MoTps1. In the MoTps1 ternary complex structure, UDP and T6P, the products of UDPG and G6P, are detected, and substantial conformational rearrangements of N-terminal domain, including structural reshuffling (β3–β4 loop to α0 helix) and movement of a ‘shift region' towards the catalytic centre, are observed. These conformational changes render MoTps1 to a ‘closed' state compared with its ‘open' state in apo or UDPG complex structures. By solving the EcOtsA apo structure, we confirmed that similar ligand binding induced conformational changes also exist in EcOtsA, although no structural reshuffling involved. Based on our research and previous studies, we present a model for the catalytic process of Tps1. Our research provides novel information on MoTps1, Tps1 family, and structure-based antifungal drug design.

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