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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.


mRNA expression level analysis (qRT-PCR) of 6 proteins of B. odoriphaga after 6 and 24 h of benzothiazole treatment.The relative expression level was normalized to an internal standard, ribosomal protein S3 (RPS3). Bars represent mean ± SE (n = 6). Different lower-case letters above the bars indicate significant differences at P < 0.05. TPI: triose-phosphate isomerase; V-ATPase: vacuolar ATP synthase subunit H; MyHC: myosin heavy chain; SCS: succinyl-CoA synthetase; ENO: enolase; epsilon BP: IgE binding protein.
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f6: mRNA expression level analysis (qRT-PCR) of 6 proteins of B. odoriphaga after 6 and 24 h of benzothiazole treatment.The relative expression level was normalized to an internal standard, ribosomal protein S3 (RPS3). Bars represent mean ± SE (n = 6). Different lower-case letters above the bars indicate significant differences at P < 0.05. TPI: triose-phosphate isomerase; V-ATPase: vacuolar ATP synthase subunit H; MyHC: myosin heavy chain; SCS: succinyl-CoA synthetase; ENO: enolase; epsilon BP: IgE binding protein.

Mentions: To determine whether gene expression is correlated between mRNA and protein levels, the following six proteins that are mainly involved in the categories of action mechanism, stress mechanism and adaption mechanism were selected for qRT-PCR analysis: triose-phosphate isomerase (TPI), vacuolar ATP synthase subunit H (V-ATPase), myosin heavy chain (MyHC), succinyl-CoA synthetase alpha (SCS), putative enolase (ENO) and putative IgE binding protein (epsilon BP). The expression levels of all selected genes encoding these proteins, with the exception of TPI, matched well with the iTRAQ results (Fig. 6). According to the qRT-PCR results, these genes had similar mRNA and protein expression patterns with similar or slightly different overall quantitative proteomics results.


Proteomic profile of the Bradysia odoriphaga in response to the microbial secondary metabolite benzothiazole
mRNA expression level analysis (qRT-PCR) of 6 proteins of B. odoriphaga after 6 and 24 h of benzothiazole treatment.The relative expression level was normalized to an internal standard, ribosomal protein S3 (RPS3). Bars represent mean ± SE (n = 6). Different lower-case letters above the bars indicate significant differences at P < 0.05. TPI: triose-phosphate isomerase; V-ATPase: vacuolar ATP synthase subunit H; MyHC: myosin heavy chain; SCS: succinyl-CoA synthetase; ENO: enolase; epsilon BP: IgE binding protein.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f6: mRNA expression level analysis (qRT-PCR) of 6 proteins of B. odoriphaga after 6 and 24 h of benzothiazole treatment.The relative expression level was normalized to an internal standard, ribosomal protein S3 (RPS3). Bars represent mean ± SE (n = 6). Different lower-case letters above the bars indicate significant differences at P < 0.05. TPI: triose-phosphate isomerase; V-ATPase: vacuolar ATP synthase subunit H; MyHC: myosin heavy chain; SCS: succinyl-CoA synthetase; ENO: enolase; epsilon BP: IgE binding protein.
Mentions: To determine whether gene expression is correlated between mRNA and protein levels, the following six proteins that are mainly involved in the categories of action mechanism, stress mechanism and adaption mechanism were selected for qRT-PCR analysis: triose-phosphate isomerase (TPI), vacuolar ATP synthase subunit H (V-ATPase), myosin heavy chain (MyHC), succinyl-CoA synthetase alpha (SCS), putative enolase (ENO) and putative IgE binding protein (epsilon BP). The expression levels of all selected genes encoding these proteins, with the exception of TPI, matched well with the iTRAQ results (Fig. 6). According to the qRT-PCR results, these genes had similar mRNA and protein expression patterns with similar or slightly different overall quantitative proteomics results.

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.