High level of resistance to proteinase inhibitors may be conferred by proteolytic cleavage in beetle larvae

Girard, Cécile; Métayer, Martine Le; Bonadé-Bottino, Michel; Pham-Delègue, M.H.; Jouanin, Lise

doi:10.1016/s0965-1748(98)00027-7

Cited by 143 publications

(94 citation statements)

References 33 publications

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“…The proteolytic enzymes are classified mainly as serine, cysteine, acid and metalloproteinase, using specific inhibitors. Acid and cysteine proteinases are predominantly detected in Coleopterans of the Bruchidae family (Lemos et al, 1990;Silva and Xavier-Filho, 1991;Girard et al, 1998;Koiwa et al, 2000), but serine proteinases are also present in other families . In general, serine proteinases are the major enzymes detected in the guts of the Lepidoptera, Hemiptera, Homoptera and Diptera orders, but acid proteinases have been isolated as well .…”

Section: Discussionmentioning

confidence: 99%

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

Silva

Alcazar

Macedo

et al. 2006

Insect Biochemistry and Molecular Biology

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The digestive system of Ceratitis capitata was characterized during its larval development and in the insect stage. Disaccharidases against maltose and sucrose were more evident in the 2nd and 3rd day of larval development and in the adult stage, respectively. Glycosil-hydrolyses with higher specific a-galactosidasic and b-galactosidasic activities were detected in the 2nd and 3rd day of the larval stage, respectively. Specific proteolytic activities against azocasein showed an increase in the 4th and 5th day of the larval stage and in the adult stage. Specific hemoglobin activities were constant between 2nd and 6th day of the larval stage. The larvae used mainly serine proteinases, such as trypsin/chymotrypsin, and the adult insects only chymotrypsin-like enzymes in their digestive process. Two serine proteinases were separated from zymogram between the 4th and 5th day of larval development and in the adult stage. Effect of soybean trypsin inhibitor (SBTI, a serine proteinase inhibitor) on development of C. capitata was examined by bioassay. C. capitata was susceptible to SBTI which affected larval mass at ED 50 3.01%. r

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Section: Discussionmentioning

confidence: 99%

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

Silva

Alcazar

Macedo

et al. 2006

Insect Biochemistry and Molecular Biology

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“…The digestive system of phytophagous pests is based mainly on serine and cysteine proteinase classes; serine proteinases are the major enzymes found in Lepidoptera and Diptera orders. Acid and cysteine proteinases are predominant in Coleopterans of the Bruchidae family [49][50][51][52], but serine proteinases are also present [53]. In order to verify the activity of purified CpaTI, the digestive proteinases of Coleopteran, Lepdopteran and Dipteran pests were extracted and assayed against BApNA, a specific trypsin substrate.…”

Section: Discussionmentioning

confidence: 99%

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

Gomes

Barbosa

Macedo

et al. 2005

Plant Physiology and Biochemistry

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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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High level of resistance to proteinase inhibitors may be conferred by proteolytic cleavage in beetle larvae

Cited by 143 publications

References 33 publications

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

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

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