Structure, dynamics, and function of PsDef2 defensin from Pinus sylvestris

Bukhteeva, Irina; Hrunyk, N. I.; Yusypovych, Yuri M.; Shalovylo, Yu. I.; Kovaleva, Valentina; Nesmelova, Irina V.

doi:10.1016/j.str.2022.03.001

Cited by 8 publications

(5 citation statements)

References 72 publications

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“…42 The defensin PsDef2 from Pinus sylvestris presents antifungal activity against Fusarium sporotrichiella and Saccharomyces cerevisiae, oomycota against Phytophthora gonapodyides and antibacterial activity; in addition, it presents inhibition of different ⊍-amylases of insects. 43 BraDef (BraDef1 + BraDef2), another plant defensin, at 12.6 μg, reduced the hyphal growth of C. gloeosporioides by approximately 56% and caused membrane disruption. 44 Understanding the mechanism of action requires an understanding of the processes that occur during growth suppression.…”

Section: Discussionmentioning

confidence: 99%

“…Defensins, LTPs, and protease inhibitors are examples of AMPs that have strong antifungal activity against fungi that infect plants, as well as other biological functions such as enzyme inhibition 42 . The defensin PsDef2 from Pinus sylvestris presents antifungal activity against Fusarium sporotrichiella and Saccharomyces cerevisiae , oomycota against Phytophthora gonapodyides and antibacterial activity; in addition, it presents inhibition of different α‐amylases of insects 43 . BraDef (BraDef1 + BraDef2), another plant defensin, at 12.6 μg, reduced the hyphal growth of C. gloeosporioides by approximately 56% and caused membrane disruption 44 …”

Section: Discussionmentioning

confidence: 99%

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Defensin‐like peptides from Capsicum chinense induce increased ROS, loss of mitochondrial functionality, and reduced growth of the fungus Colletotrichum scovillei

Resende,

de Oliveira Mello,

Zeraik

et al. 2024

Pest Management Science

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In the present study, we identified and characterized two defensin‐like peptides in an antifungal fraction obtained from Capsicum chinense pepper fruits and inhibited the growth of Colletotrichum scovillei, which causes anthracnose. AMPs were extracted from the pericarp of C. chinense peppers and subjected to ion exchange, molecular exclusion, and reversed‐phase in a high‐performance liquid chromatography system. We investigated the endogenous increase in reactive oxygen species (ROS), the loss of mitochondrial functioning, and the ultrastructure of hyphae. The peptides obtained from the G3 fraction through molecular exclusion chromatography were subsequently fractionated using reverse‐phase chromatography, resulting in the isolation of fractions F1, F2, F3, F4, and F5. The F1 fraction suppressed C. scovillei growth by 90, 70.4, and 44% at 100, 50, and 25 μg/mL, respectively. At 24 h, the IC50 and minimum inhibitory concentration were 21.5 μg/mL and 200 μg/mL, respectively. We found an increase in ROS, which may have resulted in an oxidative burst, loss of mitochondrial functioning, and cytoplasm retraction, as well as an increase in autophagic vacuoles. MS/MS analysis of the F1 fraction indicated the presence of two defensin‐like proteins, and we were able to identify the expression of three defensin sequences in our C. chinense fruit extract. The F1 fraction was also found to inhibit the activity of insect α‐amylases. In summary, the F1 fraction of C. chinense exhibits antifungal activity against a major pepper pathogen that causes anthracnose. These defensin‐like compounds are promising prospects for further research into antifungal and insecticide biotechnology applications.This article is protected by copyright. All rights reserved.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Defensin‐like peptides from Capsicum chinense induce increased ROS, loss of mitochondrial functionality, and reduced growth of the fungus Colletotrichum scovillei

Resende,

de Oliveira Mello,

Zeraik

et al. 2024

Pest Management Science

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“…Amylases have been extensively sought after for use in a wide range of clinical and pharmaceutical applications, as well as in the food, detergent, textile, brewing, and distilling industries, because of their nontoxic characteristics [14,16,17]. Amylases have been characterized from almost every group of organisms, including from a wide range of eukaryotes, e.g., animals (including humans), plants, protists, and fungi, as well as from any prokaryotes and Archaea [33][34][35][36]. Fungi, in particular, have been rich sources of amylases with various desirable properties, e.g., thermal, pH, and salt stability, and have been widely used to meet current commercial needs [35,37].…”

Section: Discussionmentioning

confidence: 99%

Characterization of an α-Amylase from the Honeybee Chalk Brood Pathogen Ascosphaera apis

Li,

Liu,

Yang

et al. 2023

JoF

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The insect pathogenic fungus, Ascosphaera apis, is the causative agent of honeybee chalk brood disease. Amylases are secreted by many plant pathogenic fungi to access host nutrients through the metabolism of starch, and the identification of new amylases can have important biotechnological applications. Production of amylase by A. apis in submerged culture was optimized using the response surface method (RSM). Media composition was modeled using Box–Behnken design (BBD) at three levels of three variables, and the model was experimentally validated to predict amylase activity (R2 = 0.9528). Amylase activity was highest (45.28 ± 1.16 U/mL, mean ± SE) in media composed of 46 g/L maltose and1.51 g/L CaCl2 at a pH of 6.6, where total activity was ~11-fold greater as compared to standard basal media. The enzyme was purified to homogeneity with a 2.5% yield and 14-fold purification. The purified enzyme had a molecular weight of 75 kDa and was thermostable and active in a broad pH range (> 80% activity at a pH range of 7–10), with optimal activity at 55 °C and pH = 7.5. Kinetic analyses revealed a Km of 6.22 mmol/L and a Vmax of 4.21 μmol/mL·min using soluble starch as the substrate. Activity was significantly stimulated by Fe2+ and completely inhibited by Cu2+, Mn2+, and Ba2+ (10 mM). Ethanol and chloroform (10% v/v) also caused significant levels of inhibition. The purified amylase essentially exhibited activity only on hydrolyzed soluble starch, producing mainly glucose and maltose, indicating that it is an endo-amylase (α-amylase). Amylase activity peaked at 99.38 U/mL fermented in a 3.7 L-bioreactor (2.15-fold greater than what was observed in flask cultures). These data provide a strategy for optimizing the production of enzymes from fungi and provide insight into the α-amylase of A. apis.

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“…Plant defensins remain structurally stable at extreme temperatures and pH and are generally non-toxic to mammalian cells, making them the most promising candidate for pest management. Therefore, revealing the relationship between the structure and function of plant defensins is helpful for their application [84]. For instance, Defensin PsDef1 from gymnosperms Pinus sylvestris (Scots pine) inhibits the activity of α-amylase from pine beauty moth, Panolis flammea [85], and PsDef2 shows a stronger inhibitory effect on α-amylases from May's beetle larva, cabbage butterfly, and darkling beetle than that of PsDef1 [84].…”

Section: Insect α-Amylase Inhibitorsmentioning

confidence: 99%

“…Therefore, revealing the relationship between the structure and function of plant defensins is helpful for their application [84]. For instance, Defensin PsDef1 from gymnosperms Pinus sylvestris (Scots pine) inhibits the activity of α-amylase from pine beauty moth, Panolis flammea [85], and PsDef2 shows a stronger inhibitory effect on α-amylases from May's beetle larva, cabbage butterfly, and darkling beetle than that of PsDef1 [84]. The widespread and diverse presence of defensins in the plant kingdom suggests that these kinds of proteins may be a potential source of antimicrobial activity, with broad prospects for agricultural biotechnology and pharmaceutical applications [81].…”

Section: Insect α-Amylase Inhibitorsmentioning

confidence: 99%

Insect α-Amylases and Their Application in Pest Management

Wang,

Huang,

Cao

et al. 2023

Molecules

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Amylase is an indispensable hydrolase in insect growth and development. Its varied enzymatic parameters cause insects to have strong stress resistance. Amylase gene replication is a very common phenomenon in insects, and different copies of amylase genes enable changes in its location and function. In addition, the classification, structure, and interaction between insect amylase inhibitors and amylases have also invoked the attention of researchers. Some plant-derived amylase inhibitors have inhibitory activities against insect amylases and even mammalian amylases. In recent years, an increasing number of studies have clarified the effects of pesticides on the amylase activity of target and non-target pests, which provides a theoretical basis for exploring safe and efficient pesticides, while the exact lethal mechanisms and safety in field applications remain unclear. Here, we summarize the most recent advances in insect amylase studies, including its sequence and characteristics and the regulation of amylase inhibitors (α-AIs). Importantly, the application of amylases as the nanocide trigger, RNAi, or other kinds of pesticide targets will be discussed. A comprehensive foundation will be provided for applying insect amylases to the development of new-generation insect management tools and improving the specificity, stability, and safety of pesticides.

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Structure, dynamics, and function of PsDef2 defensin from Pinus sylvestris

Cited by 8 publications

References 72 publications

Defensin‐like peptides from Capsicum chinense induce increased ROS, loss of mitochondrial functionality, and reduced growth of the fungus Colletotrichum scovillei

Defensin‐like peptides from Capsicum chinense induce increased ROS, loss of mitochondrial functionality, and reduced growth of the fungus Colletotrichum scovillei

Characterization of an α-Amylase from the Honeybee Chalk Brood Pathogen Ascosphaera apis

Insect α-Amylases and Their Application in Pest Management

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