期刊
PLANT CELL REPORTS
卷 30, 期 1, 页码 101-112出版社
SPRINGER
DOI: 10.1007/s00299-010-0948-z
关键词
Cysteine protease; Phytocystatin; Spider mite; Transgenic maize; Tetranychus urticae; Brevipalpus chilensis
资金
- Spanish Ministerio de Ciencia e Innovacion [BFU2008-01166]
- Agencia Espanola de Cooperacion Internacional para el Desarrollo [A/023680/09]
- Spanish Ministerio de Medioambiente y Medio Rural y Marino
Phytocystatins are inhibitors of cysteine-proteases from plants putatively involved in plant defence based on their capability of inhibit heterologous enzymes. We have previously characterised the whole cystatin gene family members from barley (HvCPI-1 to HvCPI-13). The aim of this study was to assess the effects of barley cystatins on two phytophagous spider mites, Tetranychus urticae and Brevipalpus chilensis. The determination of proteolytic activity profile in both mite species showed the presence of the cysteine-proteases, putative targets of cystatins, among other enzymatic activities. All barley cystatins, except HvCPI-1 and HvCPI-7, inhibited in vitro mite cathepsin L- and/or cathepsin B-like activities, HvCPI-6 being the strongest inhibitor for both mite species. Transgenic maize plants expressing HvCPI-6 protein were generated and the functional integrity of the cystatin transgene was confirmed by in vitro inhibitory effect observed against T. urticae and B. chilensis protein extracts. Feeding experiments impaired on transgenic lines performed with T. urticae impaired mite development and reproductive performance. Besides, a significant reduction of cathepsin L-like and/or cathepsin B-like activities was observed when the spider mite fed on maize plants expressing HvCPI-6 cystatin. These findings reveal the potential of barley cystatins as acaricide proteins to protect plants against two important mite pests.
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