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Published on: August 23, 2018
Binding proteins of destruxin A from Metarhizium against insect cell
Jingjing Wang1,2, Qunfang Weng1, Ke Zhang1
1National Key Laboratory of Green Pesticide; Key Laboratory of Natural Pesticide and Chemical Biology, Ministry of Education, College of Plant Protection, South China Agricultural University, Guangzhou, 510642, China.
Abstract:
Destruxin A (DA) is a cyclo-hexadepsipeptidic insecticidal mycotoxin isolated from the entomopathogenic fungi, Metarhizium spp. However, its mode of action is unknown. In this study, we isolated 149 candidate DA-binding proteins by drug affinity response target stability, and determined the interactions of 80 canditates with DA in vitro by surface plasmon resonance. The affinity coefficients (KD) ranged from 24 to 469 μM. Binding proteins were functionally diverse and included cytoskeletal components and cell motility, protein transcription and translation pathways, ubiquitin dependent protein metabolic processes, nucleus pore entry and exit, and endoplasmic reticulum vesicle transport and etc. Electron microscopy revealed that DA damaged the cytoskeleton and multiple organelles, disrupted cell adhesion and motility, and led to cell death. DA appeared to have a multi-targeted approach to cellular structures and multiple life processes, leading to cell death. The results of this study could provide molecular evidence for the analysis of the insecticidal toxicology of DA and further improve the study of the pathogenic insect mechanism of Metarhizium.
Insights
Destruxin A (DA), a mycotoxin from Metarhizium fungi, targets multiple cellular processes including the cytoskeleton and protein pathways. This multi-targeted action leads to cell damage and death, explaining its insecticidal effects.
Area of Science:
- Toxicology
- Mycology
- Molecular Biology
Background:
- Destruxin A (DA) is a cyclo-hexadepsipeptidic insecticidal mycotoxin from Metarhizium fungi.
- The precise mode of action for DA remains largely unknown.
Purpose of the Study:
- To identify DA-binding proteins and elucidate its molecular mechanism of action.
- To understand the cellular targets and pathways affected by DA.
Main Methods:
- Drug affinity response target stability (DARTS) was used to identify candidate DA-binding proteins.
- Surface plasmon resonance (SPR) was employed to confirm and quantify DA-protein interactions in vitro.
- Electron microscopy was utilized to observe cellular damage induced by DA.
Main Results:
- 149 candidate DA-binding proteins were isolated, with 80 confirmed to interact with DA (KD range: 24–469 μM).
- Identified binding proteins are involved in diverse cellular functions, including cytoskeletal components, cell motility, protein synthesis, and transport.
- Electron microscopy revealed DA induces cytoskeletal damage, organelle disruption, impaired cell adhesion and motility, ultimately causing cell death.
Conclusions:
- DA exhibits a multi-targeted mechanism, affecting various cellular structures and life processes.
- This study provides molecular evidence for DA's insecticidal toxicology and pathogenic mechanisms of Metarhizium.
