Characterization and distribution of digestive proteases of the stalk corn borer, Sesamia nonagrioides Lef. (Lepidoptera: Noctuidae)

Ortego, Félix; Novillo, Concepción; Castañera, Pedro

doi:10.1002/(sici)1520-6327(1996)33:2<163::aid-arch6>3.3.co;2-v

Cited by 17 publications

(26 citation statements)

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“…Transforming plant genomes with these proteinaceous protease inhibitors provide safe approach to pest control (Reckel et al, 1997). However, because of the variability of the insect proteases and the restricted range of action of the protease inhibitors (Ortego et al, 1996), the expression of a particular protease inhibitor in plants may not yield the desired result and therefore might not be an excellent candidate for biotechnology. Thus there is a continuous search for new inhibitors that are competent to combat pest adaptation.…”

Section: Introductioncontrasting

confidence: 99%

Insecticidal Potential of Abelmoschus moschatus Trypsin Inhibitor (AMTI-II) Against Mid Gut Protease of Helicoverpa armigera

Kumar¹

2017

IJASR

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Section: Introductioncontrasting

confidence: 99%

Insecticidal Potential of Abelmoschus moschatus Trypsin Inhibitor (AMTI-II) Against Mid Gut Protease of Helicoverpa armigera

Kumar¹

2017

IJASR

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“…In contrast to many other insects (Milne and Kaplan, 1993;Valaitis, 1995;Ortego et al, 1996;Novillo et al, 1999;Wagner et al, 2002) we observed low specific activities for trypsin-like and chymotrypsin-like enzymes, we have found no activity for elastolytic enzymes. The rate of breakdown of natural substrate hemoglobin by non specific proteases, probably cathepsin D-like enzymes (Lemos and Terra, 1991), was also low.…”

Section: Discussionmentioning

confidence: 99%

Peptidolytic enzymes in different larval stadium of housefly Musca domestica

Blahovec¹,

Kostecká²,

Kočišová³

2006

Vet. Med.

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Four classes of peptidolytic enzymes were described in insects. Many authors have found predominant activity belonging to trypsin-like and chymotrypsin-like activity. By the use specific chromogenic substrates and hemoglobin we have determined enzyme activity in three stages of larval development of housefly. In contrast to above mentioned data we have found, that major part of peptidolytic activity in this insect is of aminopeptidase nature. Other observed peptidolytic activity formed only minority part. Apparently the highest activities to all examined substrates were found in first larval stadium of housefly. Inhibitory studies by class specific inhibitors and influence of metal ions and chelating agent on enzyme activity have shown, that aminopeptidase-like enzymes belong to metalloproteinase group.

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“…Carboxypeptidases A and B-like activities were assayed in 0.5 mi of reaction buffer containing 20 ug of mite extracts, using 1 mM HPA (hippuryl-phenylalanine) for carboxypeptidase A-like activities and 1 mM HA (hippuryl-L-arginine) for carboxypeptidase B-like activities as described by Ortego et al (1996).…”

Section: Gelatin-page Gelsmentioning

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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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.

show abstract

Characterization and distribution of digestive proteases of the stalk corn borer, Sesamia nonagrioides Lef. (Lepidoptera: Noctuidae)

Cited by 17 publications

References 0 publications

Insecticidal Potential of Abelmoschus moschatus Trypsin Inhibitor (AMTI-II) Against Mid Gut Protease of Helicoverpa armigera

Insecticidal Potential of Abelmoschus moschatus Trypsin Inhibitor (AMTI-II) Against Mid Gut Protease of Helicoverpa armigera

Peptidolytic enzymes in different larval stadium of housefly Musca domestica

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

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