Characterization of Heat Shock Protein 60 as an Interacting Partner of Superoxide Dismutase 2 in the Silkworm, Bombyx mori, and Its Response to the Molting Hormone, 20-Hydroxyecdysone

Nojima, Yosui

doi:10.3390/antiox10091385

Cited by 6 publications

(4 citation statements)

References 47 publications

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“…persicae, similar to the findings that HSP60 interacted with SOD2 in B. mori to maintain the normal development of holometabolous insects …”

Section: Discussionsupporting

confidence: 84%

“…Additionally, the binding interaction between HSP60 and OLA1 was determined, suggesting that HSP60 might act as a chaperone in the interaction with OLA1, to maintain the function of OLA and normal development of M. persicae, similar to the findings that HSP60 interacted with SOD2 in B. mori to maintain the normal development of holometabolous insects. 56 Additionally, the coevolution between Bt and insect has been rapidly developed. Most Cry toxin contains three domains, and the interaction between Cry toxin domains and putative receptors is crucial for killing insects in a sequential binding model.…”

Section: ■ Resultsmentioning

confidence: 99%

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Protection of HSP60 in Myzus persicae Treated with Cry7Ab4 Toxin

Jin

Zhao

et al. 2023

ACS Agric. Sci. Technol.

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Heat shock proteins (HSPs) are essential for the survival and development of animals under various stresses. However, little is known about the function of HSPs in insects response to Bacillus thuringiensis (Bt) toxins treatment. Here, we investigated the role of HSP60 in Myzus persicae (M. persicae) treated with an active Cry7Ab4 toxic core. First, we demonstrated the insensitivity of M. persicae to the Cry7Ab4 toxic core through a membrane capsule method. Then, using protein pull-down assay, several putative Cry7Ab4-binding proteins, including HSP60, were identified in an M. persicae nymph. P-loop GTPase Obg-like ATPase-1 (OLA1) was also found to be a Cry2Ab12-binding protein (unpublished data). Subsequent enzymatic and RT-qPCR assays revealed that highly expressed HSP60 removed the enhanced OLA1 activity caused by Cry7Ab4. ELISA analysis confirmed the binding interactions between Cry7Ab4, HSP60, and OLA1. Interestingly, a combination of ELISA and molecular docking analysis further suggested that HSP60 could block the binding interaction between Cry7Ab4 and OLA1 via higher affinity with Cry7Ab4. Besides, the Jun N-terminal kinase (JNK) pathway was found to be activated. Overall, we proposed the model that HSP60 protects M. persicae from Cry7Ab4 toxin. The study implies that HSP60 can be a crucial factor in insect defense against Cry toxins.

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“…persicae, similar to the findings that HSP60 interacted with SOD2 in B. mori to maintain the normal development of holometabolous insects …”

Section: Discussionsupporting

confidence: 84%

Section: ■ Resultsmentioning

confidence: 99%

Protection of HSP60 in Myzus persicae Treated with Cry7Ab4 Toxin

Jin

Zhao

et al. 2023

ACS Agric. Sci. Technol.

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“…Oxidative stress promotes pupation in insects, and the level of ROS increases during metamorphosis in the silkworm fat body [35]. It increases around the fourth molt, then increases again on days 9-10 at the fth instar, just before pupation [36].…”

Section: Discussionmentioning

confidence: 99%

Characterization of a glutamate-cysteine ligase in Bombyx mori

2023

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Background: Glutamate cysteine ligase (GCL) is a crucial enzyme involved in the synthesis of glutathione (GSH). Despite various studies on glutathione transferase and its essential role in detoxi cation and resistance to oxidative stress, GSH synthesis has not been described in silkworms to date. Silkworms form part of the lepidopterans that are considered as a model of agricultural pests. This study aimed to understand the GSH synthesis through the GCL in silkworms so that insecticides can be formulated to tackle agricultural pests.Methods and Results: Based on the amino acid sequence and phylogenetic tree, this GCL belonged to group 2 and designated bmGCL. Recombinant bmGCL was overproduced and puri ed to ensure homogeneity. Biochemical studies revealed that bmGCL uses ATP and Mg 2+ to ligate glutamate and cysteine, respectively. High expression levels of bmgcl mRNA and GSH were observed in the silkworm fat body after exposure to insecticides and UV-B. Moreover, we found an increase in bmgcl mRNA and GSH content during pupation in the silkworm fat body. Conclusion:In this study, we found GCL in the silkworm Bombyx mori and its biochemical properties were investigated. These observations indicate that bmGCL might play an important role in the resistance to oxidative stress in B. mori.

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“…The interaction of prieurianin with Hsp47 would be entirely compatible with its insecticidal effects. Different chaperone proteins have been shown to play a role in the signaling of the ecdysone receptor, which is a major steroid receptor in insects [112][113][114]. Heat shock proteins play important roles in the nucleocytoplasmic shuttle of the ecdysone receptor.…”

Section: Potential Molecular Targets Of Prieurianin and Analogsmentioning

confidence: 99%

Insights into the Mechanism of Action of the Degraded Limonoid Prieurianin

Vergoten,

Bailly

2024

IJMS

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Limonoids are extremely diversified in plants, with many categories of products bearing an intact, rearranged or fragmented oxygenated scaffold. A specific subgroup of fragmented or degraded limonoids derives from the tetranortriterpenoid prieurianin, initially isolated from the tree Trichilia prieuriana but also found in other plants of the Meliaceae family, including the more abundant species Aphanamixis polystachya. Prieurianin-type limonoids include about seventy compounds, among which are dregeanin and rohitukin. Prieurianin and analogs exhibit insecticidal, antimicrobial, antiadipogenic and/or antiparasitic properties but their mechanism of action remains ill-defined at present. Previous studies have shown that prieurianin, initially known as endosidin 1, stabilizes the actin cytoskeleton in plant and mammalian cells via the modulation of the architecture and dynamic of the actin network, most likely via interference with actin-binding proteins. A new mechanistic hypothesis is advanced here based on the recent discovery of the targeting of the chaperone protein Hsp47 by the fragmented limonoid fraxinellone. Molecular modeling suggested that prieurianin and, to a lesser extent dregeanin, can form very stable complexes with Hsp47 at the protein–collagen interface. Hsp-binding may account for the insecticidal action of the product. The present review draws up a new mechanistic portrait of prieurianin and provides an overview of the pharmacological properties of this atypical limonoid and its chemical family.

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Characterization of Heat Shock Protein 60 as an Interacting Partner of Superoxide Dismutase 2 in the Silkworm, Bombyx mori, and Its Response to the Molting Hormone, 20-Hydroxyecdysone

Cited by 6 publications

References 47 publications

Protection of HSP60 in Myzus persicae Treated with Cry7Ab4 Toxin

Protection of HSP60 in Myzus persicae Treated with Cry7Ab4 Toxin

Characterization of a glutamate-cysteine ligase in Bombyx mori

Insights into the Mechanism of Action of the Degraded Limonoid Prieurianin

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