Functional Characterization of the M36 Metalloprotease FgFly1 in Fusarium graminearum

Wang, Xintong; He, Min; Liu, Huanhuan; Ding, Huiyi; Liu, Kouhan; Liu, Ying; Cheng, Peng; Li, Qiang; Wang, Baotong

doi:10.3390/jof8070726

Cited by 9 publications

(4 citation statements)

References 56 publications

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“…During the coevolution of plants and pathogens, a complex interaction relationship develops. Plants have evolved various recognition and resistance mechanisms to organize and limit pathogen infection, while pathogens have developed diverse pathogenic mechanisms to avoid or overcome plant resistance mechanisms [37]. So far, we have only confirmed that FgEps1 is involved in the pathogenesis of F. graminearum but have not yet analyzed its mode of action in this process.…”

Section: Discussionmentioning

confidence: 86%

“…Once the aerial mycelium had grown over the culture dish, the aerial mycelium was scraped off, and 500 µL of 2.5% Tween-20 solution was added. The dish was then incubated for 15 days at 25 • C, alternating between dark and light cycles every 12 h [37]. The ascospore shell and ascospore morphology were observed under the light microscope.…”

Section: Sexual Reproductionmentioning

confidence: 99%

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Protein Disulfide Isomerase FgEps1 Is a Secreted Virulence Factor in Fusarium graminearum

Liu,

Wang,

et al. 2023

JoF

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Protein disulfide isomerase (PDI) is a member of the thioredoxin (Trx) superfamily with important functions in cellular stability, ion uptake, and cellular differentiation. While PDI has been extensively studied in humans and animals, its role in fungi remains relatively unknown. In this study, the biological functions of FgEps1, a disulfide bond isomerase in the fungal pathogen Fusarium graminearum, were investigated. It was found that FgEps1 mutation affected nutritional growth, asexual and sexual reproduction, and stress tolerance. Additionally, its deletion resulted in reduced pathogenicity and impaired DON toxin biosynthesis. The involvement of FgEps1 in host infection was also confirmed, as its expression was detected during the infection period. Further investigation using a yeast signal peptide secretion system and transient expression in Nicotiana benthamiana showed that FgEps1 suppressed the immune response of plants and promoted infection. These findings suggest that virulence factor FgEps1 plays a crucial role in growth, development, virulence, secondary metabolism, and host infection in F. graminearum.

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Section: Discussionmentioning

confidence: 86%

Section: Sexual Reproductionmentioning

confidence: 99%

Protein Disulfide Isomerase FgEps1 Is a Secreted Virulence Factor in Fusarium graminearum

Liu,

Wang,

et al. 2023

JoF

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“…Among the virulence factors of phytopathogenic microorganisms, many proteins with metallopeptidase activity have been described [44][45][46][47][48][49][50][51][52][53][54]. Most of these virulencerelated metallopeptidases are considered "instruments" of brute force that contribute to the disintegration of plant tissues, providing non-specific, extensive digestion of host proteins [45,46].…”

Section: Discussionmentioning

confidence: 99%

“…Herewith, in the presence of the specific host R protein, Avr-Pita acts as a race-specific elicitor that triggers a hypersensitive response associated with full plant resistance [53]. FgFly1 metallopeptidase from Fusarium graminearum interacts with the calmodulin-binding transcription activator, inhibiting the SA-mediated immune response [54].…”

Section: Discussionmentioning

confidence: 99%

Svx Peptidases of Phytopathogenic Pectolytic Bacteria: Structural, Catalytic and Phytoimmune Properties

Tendiuk,

Diakonova,

Petrova

et al. 2024

IJMS

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Svx proteins are virulence factors secreted by phytopathogenic bacteria of the Pectobacterium genus into the host plant cell wall. Svx-encoding genes are present in almost all species of the soft rot Pectobacteriaceae (Pectobacterium and Dickeya genera). The Svx of P. atrosepticum (Pba) has been shown to be a gluzincin metallopeptidase that presumably targets plant extensins, proteins that contribute to plant cell wall rigidity and participate in cell signaling. However, the particular “output” of the Pba Svx action in terms of plant-pathogen interactions and plant immune responses remained unknown. The Svx proteins are largely unexplored in Dickeya species, even though some of them have genes encoding two Svx homologs. Therefore, our study aims to compare the structural and catalytic properties of the Svx proteins of Pba and D. solani (Dso) and to test the phytoimmune properties of these proteins. Two assayed Dso Svx proteins, similar to Pba Svx, were gluzincin metallopeptidases with conservative tertiary structures. The two domains of the Svx proteins form electronegative clefts where the active centers of the peptidase domains are located. All three assayed Svx proteins possessed phytoimmunosuppressory properties and induced ethylene-mediated plant susceptible responses that play a decisive role in Pba-caused disease.

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Zinc metalloprotease FgM35, which targets the wheat zinc-binding protein TaZnBP, contributes to the virulence of Fusarium graminearum

Wang,

Liu,

et al. 2024

Stress Biology

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Metalloproteinases are ubiquitous in organisms. Most metalloproteinases secreted by pathogenic microorganisms are also called virulence factors, because they degrade proteins in the external tissues of the host, thereby reducing the host’s immunity and increasing its susceptibility to disease. Zinc metalloproteinase is one of the most common metalloproteinases. In our report, we studied the biological function of zinc metalloprotease FgM35 in Fusarium graminearum and the pathogen–host interaction during infection. We found that the asexual and sexual reproduction of the deletion mutant ΔFgM35 were affected, as well as the tolerance of F. graminearum to metal stress. In addition, deletion of FgM35 reduced the virulence of F. graminearum. The wheat target TaZnBP was screened using a wheat yeast cDNA library, and the interaction between FgM35 and TaZnBP was verified by HADDOCK molecular docking, yeast two-hybrid, Bi-FC, Luc, and Co-IP assays. The contribution of TaZnBP to plant immunity was also demonstrated. In summary, our work revealed the indispensable role of FgM35 in the reproductive process and the pathogenicity of F. graminearum, and it identified the interaction between FgM35 and TaZnBP as well as the function of TaZnBP. This provides a theoretical basis for further study of the function of metalloproteinases in pathogen–host interactions.

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Functional Characterization of the M36 Metalloprotease FgFly1 in Fusarium graminearum

Cited by 9 publications

References 56 publications

Protein Disulfide Isomerase FgEps1 Is a Secreted Virulence Factor in Fusarium graminearum

Protein Disulfide Isomerase FgEps1 Is a Secreted Virulence Factor in Fusarium graminearum

Svx Peptidases of Phytopathogenic Pectolytic Bacteria: Structural, Catalytic and Phytoimmune Properties

Zinc metalloprotease FgM35, which targets the wheat zinc-binding protein TaZnBP, contributes to the virulence of Fusarium graminearum

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