Abstract
BackgroundThe 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.ResultsRs-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.ConclusionsOur 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.
Highlights
The nematode Radopholus similis is an important migratory endoparasite of plants
Rs-cps mRNA was expressed in the esophageal glands and ovaries of females (Fig. 3a, b, d), the esophageal glands, testes and vas deferens of males (Fig. 3f, h), and the eggs of R. similis (Fig. 3j), as indicated by hybridization with a 478-bp DIG-labeled antisense mRNA probe
The results showed that the Rs-cps mRNA transcript was present in all Effects of fluorescein isothiocyanate (FITC) and octopamine on R. similis The effects of FITC and octopamine on the activity of R. similis and the effect of octopamine on the uptake of dsRNA solution by nematodes were assessed using FITC as a visual marker
Summary
The nematode Radopholus similis is an important migratory endoparasite of plants. Cysteine protein‐ ases such as cathepsin S (CPS) play key roles during embryonic development, invasion, and pathogenesis in nema‐ todes and many other animal parasites. The burrowing nematode Radopholus similis is a migratory endoparasite of plants. R. similis is one of the most destructive plant pathogenic nematodes in the world and is listed as a quarantine pest in many countries and regions [1, 2]. Most cysteine proteases are expressed and proteolytically active in the intestines, and these enzymes are the main digestive enzymes in nematodes and animal parasites [7]. Cysteine proteinases play important roles in embryogenesis and development, infection, parasitism, pathogenesis and immune evasion in nematodes and many other animal parasites [9,10,11,12]. Nematode cysteine proteinases mainly include cathepsin B-, L-, S-, K- and Z-like cysteine proteinases, and cathepsin L (CL) and cathepsin B (CB) have been extensively
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
