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Background  The nematode  Radopholus similis  is an important migratory endoparasite of plants. Cysteine proteinases such as cathepsin S (CPS) play key roles during embryonic development, invasion, and pathogenesis in nematodes and many other animal parasites. This study was designed to investigate the molecular characterization and functions of a cathepsin S protease in  R. similis  and to find new targets for its control.    Results   Rs -CPS of  R. similis ,  Hg -CPS of  Heterodera glycines  and  Ha -CPS of  H. avenae  are closely genetically related and share the same branch of the phylogenetic tree.  Rs - cps  is a multi-copy gene that is expressed in the esophageal glands, ovaries, testes, vas deferens, and eggs of  R. similis .  Rs - cps  mRNA transcripts are expressed at varying levels during all developmental stages of  R. similis .  Rs - cps  expression was highest in females. The neurostimulant octopamine did not significantly enhance the ingestion of the dsRNA soaking solution by  R. similis  but instead had a detrimental effect on nematode activity. The dsRNA soaking solution diffused into the body of  R. similis  not only through the esophageal lumen but also through the amphids, excretory duct, vagina, anus and cloacal orifice. We confirmed that RNAi significantly suppressed the expression level of  Rs - cps  and reproductive capability and pathogenicity of  R. similis .    Conclusions  Our results demonstrate that  Rs - cps  plays important roles in the reproduction, parasitism and pathogenesis of  R. similis  and could be used as a new potential target for controlling plant parasitic nematodes.

The cathepsin S cysteine proteinase of the burrowing nematode Radopholus similis is essential for the reproduction and invasion