Tyrosine-protein phosphatase inhibitors are potentially useful for the development of products to control Meloidogyne incognita.

Meloidogyne incognita is a highly economically important plant pathogen. To contribute to the development of new products for its control, the present study aimed to: i) identify the enzymatic target of the commercial nematicide fluensulfone in the nematode in silico; and ii) determine the effects of inhibitors (or potential inhibitors according to computational calculations) of the identified enzyme on M. incognita. Searches for protein ligands three-dimensionally similar to fluensulfone, followed by molecular docking and searches for amino acid sequences in nematode genomes, suggest that the target of fluensulfone in nematodes is the enzyme tyrosine-protein phosphatase (TPP). This result was corroborated by the fact that inhibitors of this enzyme increased the immobility and mortality of M. incognita. In addition, one of the inhibitors reduced the pathogenicity of the nematode. Substances with affinities for the active site of TPP, modelled from amino acid sequences present in the genome of the free-living nematode Caenorhabditis elegans, reduced the mobility of M. incognita. Therefore, the results obtained in silico, in vitro, and in vivo demonstrate the potential of TPP inhibitors for the development of new nematicides for controlling M. incognita.