Diamondback moth (DBM), Plutella xylostella (L.), is known to be the most destructive insect of cruciferous plants. The feeding pattern of DBM on cruciferous plant has been studied by Ratzka et al. The glucosinolate sulfatase (PxGSS) that is secreted into the gut lumen of the DBM larvae enables them to feed on cruciferous plant avoiding any effect of toxic breakdown products issuing from glucosinolates (GSL) hydrolyzed by a thioglucosidase named myrosinase (MYR). The GSS removes the sulfate function of GSL that renders them invisible to MYR. The mechanism of the sulfate group removal is proposed to undergo either addition-hydrolysis or transesterification-elimination mechanisms. However, the real mechanism remains unknown due to lack of well characterized sulfatase. Although GSS has been heterologously expressed using Escherichia coli with success,Ratzka and coworkers reported the inactivation of GSS. The post-translational transformation of Cys side chain into a formylglycine (fGly) motif by FGE appeared to be critical for sulfatase activity. Therefore, the utilization of recombinant FGE from Thermomonosporal curvata (TcFGE) seems to be an optimal option to generate this post-translational modification of Cys in order to activate the PxGSS. Our approach aims to activate PxGSS using TcFGE heterologously expressed using E. coli. The enzymatic activities of activated PxGSS will be studied using different GLSs. Besides the main goal which is to assay the activation of FGE onto PxGSS, this approach could lead to a promising strategy in order to obtain a greater amount of active sulfatases heterologously expressed by E. coli.

Desulfatation of glucosinolates using glucosinolate sulfatase from xylostella plutella

2019 Spring National Meeting

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