Der p 1 and Der f 1, the highly related and major allergens from house dust mites, are differentially affected by a plant cystatin

Pernas, Mónica; Sánchez‐Ramos, Ismael; Sánchez‐Monge, Rosa; Lombardero, M.; Arteaga, C.; Castañera, Pedro; Salcedo, Gabriel

doi:10.1046/j.1365-2222.2000.00845.x

Cited by 26 publications

(21 citation statements)

References 25 publications

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“…Moreover, many other studies have shown that PhyCys also affect the growth or survival of other inseets, nematodes and slugs on artificial diets or delivered through transgenic plants (Walker et al 1999;Lilley et al 2004;Ribeiro et al 2006;Konrad et al 2009;Carrillo et al 2010). In contrast, the anti-mite properties of cystatins have only been proven using the chestnut cystatin against house dust mite species (Pernas et al 2000). In this context, the aim of the present study was to assess the putative acaricide effeets of the whole barley gene cystatin family against two phytophagous mites, T. urticae and B. chilensis, with impact on agricultural crops and to select the best cystatin as trangene to study its in vivo impact.…”

Section: Discussionmentioning

confidence: 99%

“…Deleterious effects against phytopathogenic fungi and virases have also been described for these inhibitors (Gutiérrez-Campos et al 1999;Martinez et al 2003;Abraham et al 2006). To the best of our knowledge, there is only a reference showing the acaricide properties of a phytocystatin, the CsC cystatin from chestnut (Pernas et al 2000). The CsC inhibited the crude digestive protease activity of the house dust mite Dermatophagoides farinae and drastically increased the mite larval mortality when was added to a semisynthetic diet.…”

Section: Introductionmentioning

confidence: 99%

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Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

et al. 2010

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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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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

et al. 2010

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“…The defense role has been inferred from the ability of PhyCys to inhibit digestive proteinases from herbivorous arthropods in vitro, in artificial diets as well as by bioassays on transgenic plants over-expressing PhyCys genes (Pernas et al 1998;Á lvarez-Alfageme et al 2007). Anti-mite activities and deleterious effects against phytopathogenic fungi and viruses have also been described for these inhibitors (Gutierrez-Campos et al 1999;Pernas et al 2000;Martinez et al 2003;Abraham et al 2006).…”

Section: [Lvi]-[agt]-[rke]-[fy]-[as]-[vi]-x-mentioning

confidence: 99%

A barley cysteine-proteinase inhibitor reduces the performance of two aphid species in artificial diets and transgenic Arabidopsis plants

et al. 2010

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Cystatins from plants have been implicated in plant defense towards insects, based on their role as inhibitors of heterologous cysteine-proteinases. We have previously characterized thirteen genes encoding cystatins (HvCPI-1 to HvCPI-13) from barley (Hordeum vulgare), but only HvCPI-1 C68 → G, a variant generated by direct-mutagenesis, has been tested against insects. The aim of this study was to analyze the effects of the whole gene family members of barley cystatins against two aphids, Myzus persicae and Acyrthosiphon pisum. All the cystatins, except HvCPI-7, HvCPI-10 and HvCPI-12, inhibited in vitro the activity of cathepsin L- and/or B-like proteinases, with HvCPI-6 being the most effective inhibitor for both aphid species. When administered in artificial diets, HvCPI-6 was toxic to A. pisum nymphs (LC(50) = 150 μg/ml), whereas no significant mortality was observed on M. persicae nymphs up to 1000 μg/ml. The effects of HvCPI-6 ingestion on A. pisum were correlated with a decrease of cathepsin B- and L-like proteinase activities. In the case of M. persicae, there was an increase of these proteolytic activities, but also of the aminopeptidase-like activity, suggesting that this species is regulating both target and insensitive enzymes to overcome the effects of the cystatin. To further analyze the potential of barley cystatins as insecticidal proteins against aphids, Arabidopsis plants expressing HvCPI-6 were tested against M. persicae. For A. pisum, which does not feed on Arabidopsis, a combined diet-Vicia faba plant bioassay was performed. A significant delay in the development time to reach the adult stage was observed in both species. The present study demonstrates the potential of barley cystatins to interfere with the performance of two aphid species.

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“…The defense function has been inferred from the ability of PhyCys to inhibit the activity of digestive proteases from arthropods in vitro, in artificial diets as well as through bioassays on transgenic plants overexpressing PhyCys genes (Pernas et al, 1998;Atkinson et al, 2004;Ribeiro et al, 2006;Alvarez-Alfageme et al, 2007). Anti-mite activities and deleterious effects against phytopathogenic fungi and viruses have also been described for these inhibitors (Gutierrez-Campos et al, 1999;Pernas et al, 2000;Martinez et al, 2003;Abraham et al, 2006;Wang et al, 2008).…”

Section: ([Lvi]-[agt]-[rke]-[fy]-[as]-[vi]-x-[edqv]-mentioning

confidence: 99%

Characterization of the Entire Cystatin Gene Family in Barley and Their Target Cathepsin L-Like Cysteine-Proteases, Partners in the Hordein Mobilization during Seed Germination

et al. 2009

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Plant cystatins are inhibitors of cysteine-proteases of the papain C1A and legumain C13 families. Cystatin data from multiple plant species have suggested that these inhibitors act as defense proteins against pests and pathogens and as regulators of protein turnover. In this study, we characterize the entire cystatin gene family from barley (Hordeum vulgare), which contain 13 nonredundant genes, and identify and characterize their target enzymes, the barley cathepsin L-like proteases. Cystatins and proteases were expressed and purified from Escherichia coli cultures. Each cystatin was found to have different inhibitory capability against barley cysteine-proteases in in vitro inhibitory assays using specific substrates. Real-time reverse transcriptionpolymerase chain reaction revealed that inhibitors and enzymes present a wide variation in their messenger RNA expression patterns. Their transcripts were mainly detected in developing and germinating seeds, and some of them were also expressed in leaves and roots. Subcellular localization of cystatins and cathepsin L-like proteases fused to green fluorescent protein demonstrated the presence of both protein families throughout the endoplasmic reticulum and the Golgi complex. Proteases and cystatins not only colocalized but also interacted in vivo in the plant cell, as revealed by bimolecular fluorescence complementation. The functional relationship between cystatins and cathepsin L-like proteases was inferred from their common implication as counterparts of mobilization of storage proteins upon barley seed germination. The opposite pattern of transcription expression in gibberellin-treated aleurones presented by inhibitors and enzymes allowed proteases to specifically degrade B, C, and D hordeins stored in the endosperm of barley seeds.

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Der p 1 and Der f 1, the highly related and major allergens from house dust mites, are differentially affected by a plant cystatin

Abstract: Der p 1 and Der f 1 behave very differently towards a plant cystatin, thus indicating substantial differences in their proteolytic activity. This fact could be significant with regards to the immunogenic properties of both allergens.

Cited by 26 publications

References 25 publications

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

Expression of a barley cystatin gene in maize enhances resistance against phytophagous mites by altering their cysteine-proteases

A barley cysteine-proteinase inhibitor reduces the performance of two aphid species in artificial diets and transgenic Arabidopsis plants

Characterization of the Entire Cystatin Gene Family in Barley and Their Target Cathepsin L-Like Cysteine-Proteases, Partners in the Hordein Mobilization during Seed Germination

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