ArticlePloS one2015
Inhibitory properties of cysteine protease pro-peptides from barley confer resistance to spider mite feeding.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Overexpression of soybean trypsin inhibitor genes decreases defoliation by corn earworm (Frontiers in plant science · 2023Article
- Saving time maintaining reliability: a new method for quantification of Tetranychus urticae damage in Arabidopsis whole rosettes.BMC plant biology · 2020Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2019Article
- The gut epithelium from feeding to fasting in the predatory soil mite Pergamasus longicornis (Mesostigmata: Parasitidae): one tissue, two roles.Experimental & applied acarology · 2019Review
- Arabidopsis response to the spider mite Tetranychus urticae depends on the regulation of reactive oxygen species homeostasis.Scientific reports · 2018Article
- Antixenosis and antibiosis response of common bean (Phaseolus vulgaris) to two-spotted spider mite (Tetranychus urticae).Experimental & applied acarology · 2018Article
- Indispensable Role of Proteases in Plant Innate Immunity.International journal of molecular sciences · 2018Review
- The Digestive System of the Two-Spotted Spider Mite,Frontiers in plant science · 2018Article
- Plant-Mediated Effects of Water Deficit on the Performance ofFrontiers in plant science · 2018Article
- Arabidopsis Kunitz Trypsin Inhibitors in Defense Against Spider Mites.Frontiers in plant science · 2018Article
- Drought stress promotes the colonization success of a herbivorous mite that manipulates plant defenses.Experimental & applied acarology · 2017Article
- Novel proteases from the genome of the carnivorous plant Drosera capensis: Structural prediction and comparative analysis.Proteins · 2016Article
- Enzymatic and Structural Characterization of the Major Endopeptidase in the Venus Flytrap Digestion Fluid.The Journal of biological chemistry · 2016Article
- Comparative genome-wide transcriptome analysis of Vitis vinifera responses to adapted and non-adapted strains of two-spotted spider mite, Tetranyhus urticae.BMC genomics · 2016Article
- Sequence comparison, molecular modeling, and network analysis predict structural diversity in cysteine proteases from the Cape sundew, Drosera capensis.Computational and structural biotechnology journal · 2016Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
C1A plant cysteine proteases are synthesized as pre-pro-enzymes that need to be processed to become active by the pro-peptide claves off from its cognate enzyme. These pro-sequences play multifunctional roles including the capacity to specifically inhibit their own as well as other C1A protease activities from diverse origin. In this study, it is analysed the potential role of C1A pro-regions from barley as regulators of cysteine proteases in target phytophagous arthropods (coleopteran and acari). The in vitro inhibitory action of these pro-sequences, purified as recombinant proteins, is demonstrated. Moreover, transgenic Arabidopsis plants expressing different fragments of HvPap-1 barley gene containing the pro-peptide sequence were generated and the acaricide function was confirmed by bioassays conducted with the two-spotted spider mite Tetranychus urticae. Feeding trials resulted in a significant reduction of leaf damage in the transgenic lines expressing the pro-peptide in comparison to non-transformed control and strongly correlated with an increase in mite mortality. Additionally, the analysis of the expression levels of a selection of potential mite targets (proteases and protease inhibitors) revealed a mite strategy to counteract the inhibitory activity produced by the C1A barley pro-prodomain. These findings demonstrate that pro-peptides can control mite pests and could be applied as defence proteins in biotechnological systems.
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