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1.
New Phytol ; 230(1): 275-289, 2021 04.
Article in English | MEDLINE | ID: mdl-33314087

ABSTRACT

Fusarium wilt caused by the ascomycete fungus Fusarium oxysporum is a devastating disease of many economically important crops. The mechanisms underlying plant responses to F. oxysporum infections remain largely unknown. We demonstrate here that a water-soluble, heat-resistant and nonproteinaceous F. oxysporum cell wall extract (FoCWE) component from multiple F. oxysporum isolates functions as a race-nonspecific elicitor, also termed pathogen-associated molecular pattern (PAMP). FoCWE triggers several demonstrated immune responses, including mitogen-activated protein (MAP) kinase phosphorylation, reactive oxygen species (ROS) burst, ethylene production, and stomatal closure, in cotton and Arabidopsis. Pretreated FoCWE protects cotton seeds against infections by virulent F. oxysporum f. sp. vasinfectum (Fov), and Arabidopsis plants against the virulent bacterium, Pseudomonas syringae, suggesting the potential application of FoCWEs in crop protection. Host-mediated responses to FoCWE do not appear to require LYKs/CERK1, BAK1 or SOBIR1, which are commonly involved in PAMP perception and/or signalling. However, FoCWE responses and Fusarium resistance in cotton partially require two receptor-like proteins, GhRLP20 and GhRLP31. Transcriptome analysis suggests that FoCWE preferentially activates cell wall-mediated defence, and Fov has evolved virulence mechanisms to suppress FoCWE-induced defence. These findings suggest that FoCWE is a classical PAMP that is potentially recognised by a novel pattern-recognition receptor to regulate cotton resistance to Fusarium infections.


Subject(s)
Arabidopsis , Fusarium , Cell Wall , Immunity , Plant Diseases , Plant Extracts
2.
Pest Manag Sci ; 77(2): 824-833, 2021 Feb.
Article in English | MEDLINE | ID: mdl-32926597

ABSTRACT

BACKGROUND: Fusarium fujikuroi is a plant pathogen that causes rice bakanae disease. Prochloraz is an imidazole-class sterol, 14α-demethylase inhibitor (DMI), which has been in use for several years as a foliar spray to control Fusarium spp. on agriculturally important monocot crops. F. fujikuroi is highly resistant to prochloraz treatment, and the aim of this study was to clarify the mechanism by which F. fujikuroi renders itself resistant to prochloraz. RESULTS: Recently, prochloraz-resistant strains were identified over a vast geographical area in the agricultural regions of Zhejiang Province, China. It was found that 21.13% and 3.96% of the strains examined were highly resistant (HR) to prochloraz during 2017 to 2018. The HR strains contained a point mutation (S312T) in the FfCYP51B protein, while the strains identified with prochloraz susceptibility had no such point mutation in FfCYP51A/B/C. To confirm whether the mutations in FfCYP51B confer resistance to prochloraz, we exchanged the CYP51B locus between the sensitive strain and the resistant strain by homologous double exchange. The transformed mutants with a copy of the resistant fragment exhibited resistance to prochloraz, and the transformed mutants with a copy of the sensitive fragment exhibited sensitivity to prochloraz. Furthermore, qRT-PCR analysis of Ffcyp51a/b/c gene expression revealed that Ffcyp51a and Ffcyp51b were significantly up-regulated in the prochloraz-resistant strains relative to the sensitive strains in F. fujikuroi. Contrary to our expectation, docking of prochloraz into the modeled binding pocket of FfCYP51B indicated that the affinity between prochloraz and the FfCYP51B increased after the amino acid at codon 312 changed to Thr. CONCLUSION: The point mutation S312T in FfCYP51B and overexpression of Ffcyp51a and Ffcyp51b together lead to the prochloraz-resistant phenotype in F. fujikuroi.


Subject(s)
Fungicides, Industrial , Fusarium , China , Drug Resistance, Fungal/genetics , Fungicides, Industrial/pharmacology , Fusarium/genetics , Imidazoles/pharmacology , Mutation
3.
Plant Cell ; 32(12): 3978-4001, 2020 12.
Article in English | MEDLINE | ID: mdl-33037150

ABSTRACT

Plant receptor-like kinases (RLKs) are important players in response to pathogen infections. Verticillium and Fusarium wilts, caused by Verticillium dahliae (Vd) and Fusarium oxysporum f. sp vasinfectum (Fov), respectively, are among the most devastating diseases in cotton (Gossypium spp). To understand the cotton response to these soil-borne fungal pathogens, we performed a genome-wide in silico characterization and functional screen of diverse RLKs for their involvement in cotton wilt diseases. We identified Gossypium hirsutum GhWAK7A, a wall-associated kinase, that positively regulates cotton response to both Vd and Fov infections. Chitin, the major constituent of the fungal cell wall, is perceived by lysin-motif-containing RLKs (LYKs/CERK1), leading to the activation of plant defense against fungal pathogens. A conserved chitin sensing and signaling system is present in cotton, including chitin-induced GhLYK5-GhCERK1 dimerization and phosphorylation, and contributes to cotton defense against Vd and Fov Importantly, GhWAK7A directly interacts with both GhLYK5 and GhCERK1 and promotes chitin-induced GhLYK5-GhCERK1 dimerization. GhWAK7A phosphorylates GhLYK5, which itself does not have kinase activity, but requires phosphorylation for its function. Consequently, GhWAK7A plays a crucial role in chitin-induced responses. Thus, our data reveal GhWAK7A as an important component in cotton response to fungal wilt pathogens by complexing with the chitin receptors.


Subject(s)
Ascomycota/physiology , Fusarium/physiology , Gossypium/enzymology , Plant Diseases/immunology , Plant Proteins/metabolism , Signal Transduction , Chitin/metabolism , Disease Resistance , Gossypium/genetics , Gossypium/microbiology , Host-Pathogen Interactions , Phosphorylation , Plant Diseases/microbiology , Plant Proteins/genetics
4.
Trends Plant Sci ; 25(9): 838-841, 2020 09.
Article in English | MEDLINE | ID: mdl-32576434

ABSTRACT

Although calcium (Ca2+) elevation triggered by abiotic and biotic stimuli has long been a documented phenomenon in plants, the mechanism underlying the control of Ca2+ spikes remains elusive. Recent progress, reported by Tian et al., Wang et al., Yu et al., Jiang et al., and Wu et al., has been made in elucidating how Ca2+ channels are controlled during pathogen attack, cell death, and salt or hydrogen peroxide sensing.


Subject(s)
Calcium Channels , Calcium , Calcium/metabolism , Calcium Channels/genetics , Calcium Channels/metabolism , Calcium Signaling , Plants/metabolism , Sodium Chloride
5.
Environ Pollut ; 259: 113817, 2020 Apr.
Article in English | MEDLINE | ID: mdl-31918129

ABSTRACT

2,3,3,3-Tetrafluoro-2-(heptafluoropropoxy)propanoate (known as GenX) has been used as an alternative to perfluorooctanoic acid (PFOA) which was phased out of formulations for industrial and consumer product applications in 2015. While the effects of GenX on lab animals have been studied, little is known about its effects on plants. This study examined and compared the accumulation and toxicity of GenX and PFOA in the model plants Arabidopsis thaliana and Nicotiana benthamiana. Both plants showed reduction in biomass and root growth following exposure to PFOA or GenX in a dosage-dependent manner. The bioaccumulation factors (BFs) of GenX and PFOA were plant species-dependent, with higher BFs in A. thaliana compared to N. bethanminana. Additionally, GenX and PFOA were more readily accumulated into shoot tissues of A. thaliana than in N. bethanminana. Exposure to GenX also caused a reduction in chlorophyll content (18%) and total phenolic compounds (26%). However, GenX exposure increased superoxide dismutase activity and H2O2 content (1.6 and 2.6 folds increase, respectively) in N. benthamiana. Overall, our result suggest that GenX is bioaccumulative, and that its accumulation likely inhibits plant growth and photosynthesis as well as inducing oxidative stress.


Subject(s)
Arabidopsis , Caprylates/toxicity , Fluorocarbons/toxicity , Nicotiana , Propionates/toxicity , Animals , Hydrogen Peroxide
6.
Phytopathology ; 109(10): 1679-1688, 2019 Oct.
Article in English | MEDLINE | ID: mdl-31479404

ABSTRACT

Alternative oxidase (AOX) is a ubiquinol terminal oxidase that is involved in fungal mitochondrial oxidative phosphorylation. In this study, we analyzed the roles of AOX in Botrytis cinerea by generating BcAOX deletion mutants. The mutants exhibited defects in mycelial growth, sporulation, spore germination, and virulence. Furthermore, the sensitivity of the mutants to quinone outside inhibitor fungicides and oxidative stress were increased. All phenotypic variations could be restored in the complemented strain. In summary, these results showed that BcAOX is involved in the regulation for vegetative development, adaptation to environmental stress, and virulence of B. cinerea.


Subject(s)
Botrytis , Mitochondrial Proteins , Oxidoreductases , Oxygen , Plant Proteins , Botrytis/enzymology , Botrytis/growth & development , Botrytis/pathogenicity , Mitochondrial Proteins/metabolism , Oxidative Stress/physiology , Oxidoreductases/metabolism , Plant Proteins/metabolism , Virulence
7.
Biochem J ; 475(15): 2491-2509, 2018 08 16.
Article in English | MEDLINE | ID: mdl-30115747

ABSTRACT

Plants sense the presence of pathogens or pests through the recognition of evolutionarily conserved microbe- or herbivore-associated molecular patterns or specific pathogen effectors, as well as plant endogenous danger-associated molecular patterns. This sensory capacity is largely mediated through plasma membrane and cytosol-localized receptors which trigger complex downstream immune signaling cascades. As immune signaling outputs are often associated with a high fitness cost, precise regulation of this signaling is critical. Protease-mediated proteolysis represents an important form of pathway regulation in this context. Proteases have been widely implicated in plant-pathogen interactions, and their biochemical mechanisms and targets continue to be elucidated. During the plant and pathogen arms race, specific proteases are employed from both the plant and the pathogen sides to contribute to either defend or invade. Several pathogen effectors have been identified as proteases or protease inhibitors which act to functionally defend or camouflage the pathogens from plant proteases and immune receptors. In this review, we discuss known protease functions and protease-regulated signaling processes involved in both sides of plant-pathogen interactions.


Subject(s)
Host-Pathogen Interactions/physiology , Peptide Hydrolases/metabolism , Plant Diseases , Plant Proteins/metabolism , Plants/metabolism , Proteolysis , Signal Transduction , Plants/microbiology
8.
Plant Sci ; 274: 242-251, 2018 Sep.
Article in English | MEDLINE | ID: mdl-30080610

ABSTRACT

Plant receptor-like proteins (RLPs) are a family of transmembrane receptors which are distinguished from receptor-like kinases (RLKs) by their lack of a cytoplasmic kinase domain. RLPs continue to be implicated in a broad range of plant immunological and developmental processes as critical sensors or participants in receptor complexes on the plasma membrane. RLPs often associate with RLKs to activate or attenuate signal perception and relay. Some RLPs also physically cluster with RLKs and bear similar expression patterns. Here, we discuss the characteristics, function, and expression of characterized RLPs in the context of their associated RLKs in plant immunity and development.


Subject(s)
Plant Cells/immunology , Plant Immunity , Plants/immunology , Receptors, Cell Surface/metabolism , Receptors, Pattern Recognition/metabolism , Plant Cells/metabolism , Plant Development , Plant Proteins/genetics , Plant Proteins/metabolism , Plants/metabolism , Receptors, Cell Surface/genetics , Receptors, Pattern Recognition/genetics
9.
Trends Plant Sci ; 23(5): 372-374, 2018 05.
Article in English | MEDLINE | ID: mdl-29602571

ABSTRACT

Leucine-rich repeat receptor kinases (LRR-RKs) represent a large and functionally diverse family of transmembrane proteins critical for signal recognition and transduction at the plant cell plasma membrane. Here, we discuss a recent report which used a systems-level approach to validate key paradigms by constructing an LRR-RK interaction network model.


Subject(s)
Arabidopsis , Leucine , Arabidopsis Proteins , Protein Domains , Protein Kinases
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