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

ABSTRACT:

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

SUBMITTER: Wang K 

PROVIDER: S-EPMC4901441 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature