Nematicidal effects of cysteine proteinases against sedentary plant parasitic nematodes
Stepek, Gillian; Curtis, R.H.C.; Kerry, B.R.; Shewry, P.R.; Clark, S.J.; Lowe, Ann; Duce, I.R.; Buttle, David J.; Behnke, J.M.
David J. Buttle
Cysteine proteinases from the fruit and latex of plants, such as papaya, pineapple and fig, have previously been shown to have substantial anthelmintic efficacy, in vitro and in vivo, against a range of animal parasitic nematodes. In this paper, we describe the in vitro effects of these plant extracts against 2 sedentary plant parasitic nematodes of the genera Meloidogyne and Globodera. All the plant extracts examined caused digestion of the cuticle and decreased the activity of the tested nematodes. The specific inhibitor of cysteine proteinases, E-64, blocked this activity completely, indicating that it was essentially mediated by cysteine proteinases. In vitro, plant cysteine proteinases are active against second-stage juveniles of M. incognita and M. javanica, and some cysteine proteinases also affect the second-stage juveniles of Globodera rostochiensis. It is not known yet whether these plant extracts will interfere with, or prevent invasion of, host plants.
|Journal Article Type||Article|
|Publication Date||Jan 1, 2007|
|Publisher||Cambridge University Press (CUP)|
|Peer Reviewed||Peer Reviewed|
|APA6 Citation||Stepek, G., Curtis, R., Kerry, B., Shewry, P., Clark, S., Lowe, A., …Behnke, J. (2007). Nematicidal effects of cysteine proteinases against sedentary plant parasitic nematodes. Parasitology, 134(12), doi:10.1017/S0031182007003289|
|Keywords||plant parasitic nematodes, Meloidogyne spp., Globodera rostochiensis, plant cysteine proteinases, in vitro, nematicide|
|Copyright Statement||Copyright information regarding this work can be found at the following address: http://eprints.nottingh.../end_user_agreement.pdf|
|Additional Information||Copyright Cambridge University Press.|
Stepek et al 2007 Parasitology 134, 1831 plant parasitic nematodes.pdf
Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf