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Proteomic profile of the Bradysia odoriphaga in response to the microbial secondary metabolite benzothiazole

View Article: PubMed Central - PubMed

ABSTRACT

Benzothiazole, a microbial secondary metabolite, has been demonstrated to possess fumigant activity against Sclerotinia sclerotiorum, Ditylenchus destructor and Bradysia odoriphaga. However, to facilitate the development of novel microbial pesticides, the mode of action of benzothiazole needs to be elucidated. Here, we employed iTRAQ-based quantitative proteomics analysis to investigate the effects of benzothiazole on the proteomic expression of B. odoriphaga. In response to benzothiazole, 92 of 863 identified proteins in B. odoriphaga exhibited altered levels of expression, among which 14 proteins were related to the action mechanism of benzothiazole, 11 proteins were involved in stress responses, and 67 proteins were associated with the adaptation of B. odoriphaga to benzothiazole. Further bioinformatics analysis indicated that the reduction in energy metabolism, inhibition of the detoxification process and interference with DNA and RNA synthesis were potentially associated with the mode of action of benzothiazole. The myosin heavy chain, succinyl-CoA synthetase and Ca+-transporting ATPase proteins may be related to the stress response. Increased expression of proteins involved in carbohydrate metabolism, energy production and conversion pathways was responsible for the adaptive response of B. odoriphaga. The results of this study provide novel insight into the molecular mechanisms of benzothiazole at a large-scale translation level and will facilitate the elucidation of the mechanism of action of benzothiazole.

No MeSH data available.


Experimental design and schematic diagram of the workflow of this study.CON: control, BT: benzothiazole.
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f2: Experimental design and schematic diagram of the workflow of this study.CON: control, BT: benzothiazole.

Mentions: Figure 2 shows the workflow of iTRAQ-based quantitative proteomic analysis and some proteins that were verified by qRT-PCR in this study. A total of 863 proteins were identified on the basis of 9,145 highly confident spectra, of which 1,552 peptides were unique (Fig. 3A). In terms of protein mass distribution, good coverage was obtained for a wide range for proteins larger than 10‚ÄČkDa (Fig. 3B).


Proteomic profile of the Bradysia odoriphaga in response to the microbial secondary metabolite benzothiazole
Experimental design and schematic diagram of the workflow of this study.CON: control, BT: benzothiazole.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC5121901&req=5

f2: Experimental design and schematic diagram of the workflow of this study.CON: control, BT: benzothiazole.
Mentions: Figure 2 shows the workflow of iTRAQ-based quantitative proteomic analysis and some proteins that were verified by qRT-PCR in this study. A total of 863 proteins were identified on the basis of 9,145 highly confident spectra, of which 1,552 peptides were unique (Fig. 3A). In terms of protein mass distribution, good coverage was obtained for a wide range for proteins larger than 10‚ÄČkDa (Fig. 3B).

View Article: PubMed Central - PubMed

ABSTRACT

Benzothiazole, a microbial secondary metabolite, has been demonstrated to possess fumigant activity against Sclerotinia sclerotiorum, Ditylenchus destructor and Bradysia odoriphaga. However, to facilitate the development of novel microbial pesticides, the mode of action of benzothiazole needs to be elucidated. Here, we employed iTRAQ-based quantitative proteomics analysis to investigate the effects of benzothiazole on the proteomic expression of B. odoriphaga. In response to benzothiazole, 92 of 863 identified proteins in B. odoriphaga exhibited altered levels of expression, among which 14 proteins were related to the action mechanism of benzothiazole, 11 proteins were involved in stress responses, and 67 proteins were associated with the adaptation of B. odoriphaga to benzothiazole. Further bioinformatics analysis indicated that the reduction in energy metabolism, inhibition of the detoxification process and interference with DNA and RNA synthesis were potentially associated with the mode of action of benzothiazole. The myosin heavy chain, succinyl-CoA synthetase and Ca+-transporting ATPase proteins may be related to the stress response. Increased expression of proteins involved in carbohydrate metabolism, energy production and conversion pathways was responsible for the adaptive response of B. odoriphaga. The results of this study provide novel insight into the molecular mechanisms of benzothiazole at a large-scale translation level and will facilitate the elucidation of the mechanism of action of benzothiazole.

No MeSH data available.