Are insects resistant to plant proteinase inhibitors?

Broadway, Roxanne M.

doi:10.1016/0022-1910(94)00101-l

Cited by 236 publications

(161 citation statements)

References 25 publications

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“…There are numerous classes of naturally occurring phytochemicals that are thought to confer resistance to plants against herbivorous insects. These classes include lectins, waxes, phenolics, sugars, alpha-amylase inhibitors and proteinase inhibitors (Broadway, 1995). Analysis of sugarcane-expressed genes involved in secondary metabolism suggests that most of the expressed compounds may be acting as defensive barriers to insect attack (Table I, Figure 2).…”

Section: Resultsmentioning

confidence: 99%

Mechanisms of sugarcane response to herbivory

et al. 2001

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Deciphering plant-insect interactions at the molecular level is one of the major topics of interest in contemporary plant biology research. In the last few years, various aspects of the plant response to insect damage have been investigated, including the characterization of direct and indirect responses, the regulation of gene expression resulting from insect attack and the signal transduction pathways. Such research has resulted in the proposal of new methods to enhance host resistance to insect pests, including the use of insecticidal genes that can be transferred by genetic engineering into target crops. By integrating the understanding of how plants react to insect damage with the techniques of molecular biology researchers should be able to increase the wide range of methods available for the control of insect pests. The sugarcane transcriptome project (SUCEST) has allowed the identification of several orthologues genes involved in the plant response to insect damage. In this paper we summarize several aspects of the complex interaction between plants and insects and describe the use of in silico analysis to provide information about gene expression in different sugarcane tissues in response to insect attack.

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Section: Resultsmentioning

confidence: 99%

Mechanisms of sugarcane response to herbivory

et al. 2001

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“…The necessity of such a strategy has become increasingly evident with the understanding that many insects possess very effective resistance mechanisms against individual PIs. Resistance has been attributed to complex proteolytic systems, allowing the insects to degrade PIs in Coleoptera (Girard et al, 1998a) and Lepidoptera (Giri et al, 1998), and to enhance the production of inhibitor-insensitive proteinases in response to PI ingestion in Coleoptera (Girard et al, 1998b;Bonade-Bottino et al, 1999;Cloutier et al, 1999) and Lepidoptera (Broadway 1995(Broadway , 1997Jongsma et al, 1995;Broadway, 1996b;Brown et al, 1997;Wu et al, 1997). It has been suggested (Orr et al, 1994;Broadway, 1996a) that such complex mechanisms are most likely to exist in polyphagous insects having generalized feeding habits compared to oligo-or monophagous insects.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of cysteine and aspartyl proteinases in the alfalfa weevil midgut with biochemical and plant-derived proteinase inhibitors

Wilhite

Elden

Brzin

et al. 2000

Insect Biochemistry and Molecular Biology

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"Inhibition of cysteine and aspartyl proteinases in the alfalfa weevil midgut with biochemical and plant-derived proteinase inhibitors" (2000). AbstractProteolytic activities in alfalfa weevil (Hypera postica) larval midguts have been characterized. Effects of pH, thiol activators, low-molecular weight inhibitors, and proteinase inhibitors (PIs) on general substrate hydrolysis by midgut extracts were determined. Hemoglobinolytic activity was highest in the acidic to mildly acidic pH range, but was maximal at pH 3.5. Addition of thiolactivators dithiothreitol (DTT), 2-mercaptoethanol (2-ME), or l-cysteine had little effect on hemoglobin hydrolysis at pH 3.5, but enhanced azocaseinolytic activity two to three-fold at pH 5.0. The broad cysteine PI E-64 reduced azocaseinolytic activity by 64% or 42% at pH 5 in the presence or absence of 5 mM l-cysteine, respectively. Inhibition by diazomethyl ketones, Z-Phe-Phe-CHN 2 and Z-Phe-Ala-CHN 2 , suggest that cathepsins L and B are present and comprise approximately 70% and 30% of the cysteine proteolytic activity, respectively. An aspartyl proteinase component was identified using pepstatin A, which inhibited 32% (pH 3.5, hemoglobin) and 50% (pH 5, azocasein) of total proteolytic activity. This activity was completely inhibited by an aspartyl proteinase inhibitor from potato (API), and is consistent with the action of a cathepsin D-like enzyme. Hence, genes encoding PIs with specificity toward cathepsins L, B and D could potentially be effective for control of alfalfa weevil using transgenic plants.

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“…As a consequence, a wide range of investigations have been focused on the characterisation and identification of different target proteinases in a variety of insect orders: Lepidoptera, such as Agrotis (Purcell et al, 1992), Cydia (Christeller et al, 1992), Spodoptera (Lee and Anstee, 1995), Lymantria (Valaitis, 1995), Heliothis (Johnston et al, 1995), Ostrinia (Bernardi et al, 1996), Bombyx (Nobuyasu and Yamashita, 1997), Sesamia (Novillo et al, 1999), Pieris (Broadway, 1995); in Coleoptera, such as Adalia (Murdock et al, 1987;Walker et al, 1998), Tenebrio (Dadd, 1956;Jang et al, 1998) and Tribolium (BlancoLabra et al, 1996); in Diptera, such as Aedes (Fisk, 1950) and Aenopheles (Berner et al, 1983;Vizioli et al, 2001); in Hemiptera, such as Dysdercus (Khan and Ford, 1962); and in Orthoptera, such as Locusta (Khan, 1963). The potential damage of protein-inhibitors on the digestive proteinases of beneficial insects has received less attention.…”

Section: Introductionmentioning

confidence: 99%

Expression profile of water-soluble proteinases during ontogenesis of Megachile rotundata: an electrophoretic investigation

et al. 2004

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-Variations in proteinase activity pattern in larva, pupa and imago of the solitary bee Megachile rotundata are described. Extraction of insect homogenates under mild conditions was followed by the electrophoretic separation of the protein extract in polyacrylamide gels, precast with either gelatine or pollen protein extracts. In these conditions, twelve distinct proteinases were detectable in the pooled I-IV instar larvae, six in the pollen-eating V instar, two in the mature V instar, none in the diapausing V instar, none in the pupa, and two in the imago. Some of the detected proteinases were able to digest the protein mixture extracted from the pollen provisions. Some proteinases were insect specific since they were not detectable in pollen provisions extract. The enzymologic properties of the major proteolytic band suggest its serine-proteinase nature.solitary bee / Megachile rotundata / development / proteinase / zymography

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Are insects resistant to plant proteinase inhibitors?

Cited by 236 publications

References 25 publications

Mechanisms of sugarcane response to herbivory

Mechanisms of sugarcane response to herbivory

Inhibition of cysteine and aspartyl proteinases in the alfalfa weevil midgut with biochemical and plant-derived proteinase inhibitors

Expression profile of water-soluble proteinases during ontogenesis of Megachile rotundata: an electrophoretic investigation

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