Protease Inhibitors: An Induced Plant Defense Mechanism Against Herbivores

Divekar, Pratap A.; Rani, Vijaya; Majumder, Sujan; Karkute, Suhas Gorakh; Molla, Kutubuddin A.; Pandey, Koshlendra Kumar; Behera, Tusar Kanti; Pandi, G. Guru Pirasanna

doi:10.1007/s00344-022-10767-2

Cited by 17 publications

(14 citation statements)

References 114 publications

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“…Differential protein abundance can be the result of several processes including changes in de novo protein biosynthesis, protein modification and protein degradation. Protease and protease inhibitors are common regulators for those changes during plant response to abiotic and biotic stresses (Thomas and van der Hoorn, 2018; Sharma and Gayen, 2021; Divekar et al, 2022). In this study, we identified a total of 31 cold-induced proteases mainly including the specific ATP-dependent Clp proteases, cysteine proteases and non-specific ones such as the serine proteases and aspartyl proteases (Table S2).…”

Section: Resultsmentioning

confidence: 99%

“…Notably, the upregulated ASP is homologous to the AtKTI5 (At1g17860.1), a member of the Kunitz trypsin inhibitor (KTI) family. KTI protease inhibitors have been found to be involved in plant immunity and stress resistance by regulating protease activity (Brzin and Kidric, 1996; Divekar et al, 2022). Taken together, we hypothesized that the cold-induced ASP could be one of a key players modulating freezing tolerance at the proteomic level in kumquat.…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, we identified a cold-induced protease inhibitor FmASP in proteomics study and characterized its function. Protease inhibitor are multifunctional proteins implicated in the control of endogenous proteolysis under biotic and abiotic stress conditions (Brzin and Kidric, 1996; Divekar et al, 2022). Constitutive expression of protease inhibitors has been shown to enhance the stress response and tolerance in plants (Huang et al, 2007; Srinivasan et al, 2009; Tiwari et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

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Protease inhibitor ASP enhances freezing tolerance by inhibiting protein degradation in Kumquat

Yang

Qiao

Teng

et al. 2022

Preprint

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Cold acclimation is a complex biological process leading to the development of freezing tolerance in plants. In this study, we demonstrated that cold-induced expression of protease inhibitor FmASP in a citrus relative species kumquat (Fortunella margarita (Lour.) Swingle) contributes to its freezing tolerance by regulating protein degradation. First, we found that only cold-acclimated kumquat plants, although with extensive leaf cellular damage during freezing, are able to resume their normal growth upon stress relief. To dissect the impact of cold acclimation on this extraordinary freezing tolerance, we performed protein abundance assay and quantitative proteomics analysis of kumquat leaves subjected to cold acclimation (4 °C), freezing treatment (−10 °C) and post-stress recovery (25 °C). FmASP and a few non-specific proteases were identified as differentially expressed proteins induced by cold acclimation and associated with stable protein abundance throughout the course of freezing treatment. FmASP was further characterized as a robust inhibitor that inhibits the degradation capacity of multiple proteases. In addition, heterogeneous expression of FmASP in Arabidopsis confirmed its positive function in freezing tolerance. Finally, we proposed a working model of FmASP and illustrated how this extracellular-localized protease inhibitor protects proteins from degradation and consequently maintains essential cellular function for freezing stress recovery. These findings revealed the important role of protease inhibition on freezing response and provide insights on how this role may help develop new strategies to enhance plant freezing tolerance.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Protease inhibitor ASP enhances freezing tolerance by inhibiting protein degradation in Kumquat

Yang

Qiao

Teng

et al. 2022

Preprint

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“…However, the cultivars exhibiting the highest resistance do not necessarily possess the highest level of scopoletin. This observation is reasonable since the search for metabolically effective compounds with disease resistance effects should acknowledge the presence of various other phytoprotectants in plants, such as ipomeamarone and other terpenoids; the role of defense proteins and H 2 O 2 should also not be ignored. , Collectively, the concerted action of rapidly accumulated and diverse disease-resistant compounds and defense proteins in plants is essential for shaping the strongest disease resistance.…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis of Scopoletin in Sweet Potato Confers Resistance against Fusarium oxysporum

Wang,

Chen,

Zhao

et al. 2024

J. Agric. Food Chem.

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Fusarium wilt is a severe fungal disease caused by Fusarium oxysporum in sweet potato. We conducted transcriptome analysis to explore the resistance mechanism of sweet potato against F. oxysporum. Our findings highlighted the role of scopoletin, a hydroxycoumarin, in enhancing resistance. In vitro experiments confirmed that scopoletin and umbelliferone had inhibitory effects on the F. oxysporum growth. We identified hydroxycoumarin synthase genes IbF6′H2 and IbCOSY that are responsible for scopoletin production in sweet potatoes. The co-overexpression of IbF6′H2 and IbCOSY in tobacco plants produced the highest scopoletin levels and disease resistance. This study provides insights into the molecular basis of sweet potato defense against Fusarium wilt and identifies valuable genes for breeding wilt-resistant cultivars.

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“…The intake of PIs is known to impede insect gut digestion, leading to reduced nutrient uptake and amino acid deficiency. This, in turn, leads to developmental delay and reduced fecundity [51]. Moreover, LOX activity might further aggravate the nutritional deficiency of host plants [52].…”

Section: Discussionmentioning

confidence: 99%

Combined Jasmonic Acid and Ethylene Treatment Induces Resistance Effect in Faba Bean Plants Against Frankliniella occidentalis (Pergande) (Thysanoptera: Thripidae)

Jia

Zhang

JunRui

et al. 2022

Insects

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Frankliniella occidentalis (Pergande) (Thysanoptera: Thripidae) is a serious invasive pest in China. In this study, we determined whether exogenous jasmonic acid (JA) and ethylene (ET) treatments could induce resistance against F. occidentalis in faba bean plants. First, we investigated the effects of different concentrations of JA or ET alone on F. occidentalis and then assessed the effects of optimal concentrations of JA and ET combined. Our results showed that the optimal concertation of JA was 2 mmol/L and ET was 0.5 mmol/L. JA + ET mixture showed the greatest inhibitory effect in terms of oviposition and feeding. JA with ET was found to induce changes in the activities of lipoxygenase (LOX), allene oxide synthase (AOS), polyphenol oxidase (PPO), 1-aminocyclopropane 1-carboxylic acid synthase (ACS), and trypsin inhibitor (TI). This treatment also activated or inhibited the relative expression levels of LOX1, ACO2, ACS2, and AP2/ERF. Treatment of faba bean plants with JA and ET significantly prolonged F. occidentalis development and adult preoviposition period, significantly reduced per-female oviposition, and altered male longevity and offspring demographic parameters. These results indicate that JA with ET can induce defenses against the growth and development of F. occidentalis in faba bean plants.

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Protease Inhibitors: An Induced Plant Defense Mechanism Against Herbivores

Cited by 17 publications

References 114 publications

Protease inhibitor ASP enhances freezing tolerance by inhibiting protein degradation in Kumquat

Protease inhibitor ASP enhances freezing tolerance by inhibiting protein degradation in Kumquat

Biosynthesis of Scopoletin in Sweet Potato Confers Resistance against Fusarium oxysporum

Combined Jasmonic Acid and Ethylene Treatment Induces Resistance Effect in Faba Bean Plants Against Frankliniella occidentalis (Pergande) (Thysanoptera: Thripidae)

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