Identification of a wheat polygalacturonase-inhibiting protein involved in Fusarium head blight resistance

Hou, Wenqian; Mu, Jingjing; Li, Anfei; Wang, Hong Wei; Kong, Lingrang

doi:10.1007/s10658-014-0574-7

Cited by 21 publications

(12 citation statements)

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“…This possibility, which deserves further investigation, is also supported by the finding that the wheat tissue contains PG-inhibiting proteins with N-terminal sequences (Lin and Li, 2002 ; Kemp et al, 2003 ) different from TaPGIP1 and TaPGIP2 (Janni et al, 2013 ) and from the pgip sequences reported so far ( http://www.ncbi.nlm.nih.gov/nucleotide/ ). Recently, a wheat gene with some sequence similarity to pgip genes has been reported and was shown to be involved in the defense response against Fusarium graminearum (Hou et al, 2014 ).…”

Section: Inhibition Activity Of Pgipsmentioning

confidence: 99%

An update on polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein that protects crop plants against pathogens

et al. 2015

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Polygalacturonase inhibiting proteins (PGIPs) are cell wall proteins that inhibit the pectin-depolymerizing activity of polygalacturonases secreted by microbial pathogens and insects. These ubiquitous inhibitors have a leucine-rich repeat structure that is strongly conserved in monocot and dicot plants. Previous reviews have summarized the importance of PGIP in plant defense and the structural basis of PG-PGIP interaction; here we update the current knowledge about PGIPs with the recent findings on the composition and evolution of pgip gene families, with a special emphasis on legume and cereal crops. We also update the information about the inhibition properties of single pgip gene products against microbial PGs and the results, including field tests, showing the capacity of PGIP to protect crop plants against fungal, oomycetes and bacterial pathogens.

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Section: Inhibition Activity Of Pgipsmentioning

confidence: 99%

An update on polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein that protects crop plants against pathogens

et al. 2015

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“…To identify the biological pathway information of F. moniliforme in response to Phloridzin inducers, these 293 proteins were further mapped to the corresponding pathways included in the KEGG database. These 293 dehydrogenase 1, L-lactate dehydrogenase also upregulated, L-lactate dehydrogenase is a key enzyme that produces lactic and phenyllactate [44]. β-1,4-xylanase is a key enzyme in the process of xylan degradation.…”

Section: Discussionmentioning

confidence: 99%

ITRAQ-based quantitative proteomic analysis of Fusarium moniliforme (Fusarium verticillioides) in response to Phloridzin inducers

et al. 2021

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Background Apple replant disease (ARD) has been reported from all major fruit-growing regions of the world, and is often caused by biotic factors (pathogen fungi) and abiotic factors (phenolic compounds). In order to clarify the proteomic differences of Fusarium moniliforme under the action of phloridzin, and to explore the potential mechanism of F. moniliforme as the pathogen of ARD, the role of Fusarium spp. in ARD was further clarified. Methods In this paper, the quantitative proteomics method iTRAQ analysis technology was used to analyze the proteomic differences of F. moniliforme before and after phloridzin treatment. The differentially expressed protein was validated by qRT-PCR analysis. Results A total of 4535 proteins were detected, and 293 proteins were found with more than 1.2 times (P< 0.05) differences. In-depth data analysis revealed that 59 proteins were found with more than 1.5 times (P< 0.05) differences, and most proteins were consistent with the result of qRT-PCR. Differentially expressed proteins were influenced a variety of cellular processes, particularly metabolic processes. Among these metabolic pathways, a total of 8 significantly enriched KEGG pathways were identified with at least 2 affiliated proteins with different abundance in conidia and mycelium. Functional pathway analysis indicated that up-regulated proteins were mainly distributed in amino sugar, nucleotide sugar metabolism, glycolysis/ gluconeogenesis and phagosome pathways. Conclusions This study is the first to perform quantitative proteomic investigation by iTRAQ labeling and LC-MS/MS to identify differentially expressed proteins in F. moniliforme under phloridzin conditions. The results confirmed that F. moniliforme presented a unique protein profile that indicated the adaptive mechanisms of this species to phloridzin environments. The results deepened our understanding of the proteome in F. moniliforme in response to phloridzin inducers and provide a basis for further exploration for improving the efficiency of the fungi as biocontrol agents to control ARD.

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“…In this study, the large expression of phosphoenolpyruvate carboxykinase and 5-gluconate dehydrogenase in F. moniliforme under the phloridzin environment is helpful to promote the gluconeogenesis pathway in F. moniliforme Amino acid metabolism and carbohydrate metabolism. In addition, 3-methyl-2-oxobutanoate hydroxymethyltransferase, phosphopantothenoylcysteine decarboxylase, acyl-CoA dehydrogenase, triosephosphate isomerase, related to beta-1,4-mannosyltransferase, related to gamma-glutamyltransferase, alcohol dehydrogenase 1, L-lactate dehydrogenase also up-regulated, L-lactate dehydrogenase is a key enzyme that produces lactic and phenyllactate (Hou et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

ITRAQ-based quantitative proteomic analysis of Fusarium moniliforme (Fusarium verticillioides) in response to Phloridzin inducers

Zhang

Jiang

Liu

et al. 2020

Preprint

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Apple replant disease (ARD) has been reported from all major fruit-growing regions of the world, and is often caused by biotic factors (pathogen fungi) and abiotic factors (phenolic compounds). In order to clarify the proteomic differences of Fusarium moniliforme under the action of phloridzin, and to explore the potential mechanism of F. moniliforme as the pathogen of ARD, the role of Fusarium spp in ARD was further clarified. In this paper, the quantitative proteomics method iTRAQ analysis technology was used to analyze the proteomic differences of F. moniliforme before and after phloridzin treatment. A total of 4535 proteins were detected, and 293 proteins were found with more than 1.2 times (P<0.05) differences. In-depth data analysis revealed that differentially expressed proteins were influenced a variety of cellular processes, particularly metabolic processes. Among these metabolic pathways, a total of 8 significantly enriched KEGG pathways were identified with at least 2 affiliated proteins with different abundance in conidia and mycelium. Functional pathway analysis indicated that 46 up-regulated proteins were mainly distributed in amino sugar, nucleotide sugar metabolism, glycolysis/ gluconeogenesis and phagosome pathways. The results deepened our understanding of the proteome in F. moniliforme in response to phloridzin inducers and provide a basis for further exploration for improving the efficiency of the fungi as biocontrol agents to control ARD.

show abstract

Identification of a wheat polygalacturonase-inhibiting protein involved in Fusarium head blight resistance

Cited by 21 publications

References 59 publications

An update on polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein that protects crop plants against pathogens

An update on polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat protein that protects crop plants against pathogens

ITRAQ-based quantitative proteomic analysis of Fusarium moniliforme (Fusarium verticillioides) in response to Phloridzin inducers

ITRAQ-based quantitative proteomic analysis of Fusarium moniliforme (Fusarium verticillioides) in response to Phloridzin inducers

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