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Exp Parasitol. 2007 Feb;115(2):114-20. Epub 2006 Sep 22.

Meloidogyne incognita: molecular and biochemical characterisation of a cathepsin L cysteine proteinase and the effect on parasitism following RNAi.

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Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, UK.


RNA interference has been used to investigate the function of a cathepsin L cysteine proteinase Mi-cpl-1, in the plant-parasitic nematode Meloidogyne incognita. A reduction in gene transcript was observed and the number of nematodes infecting plants was reduced by almost 60% as was the number of established females producing eggs at 21 days post-infection. The cysteine proteinase activity of M. incognita, reported by the substrate GLUpNA, was inhibited by the cysteine proteinase inhibitor Oc-IDeltaD86. A reduction in cysteine proteinase activity was also seen following RNAi of Mi-cpl-1 in J2 stage nematodes. In situ hybridization analysis in young and mature female nematodes has shown that Mi-cpl-1 is expressed in the intestine, which suggests that its product is a digestive enzyme. The effects of knocking-out Mi-cpl-1gene function were consistent with a reduction in feeding efficiency. Here, we have shown a correlation between transcript abundance proteinase activity and parasitic success of M. incognita.

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