Identification of novel serine proteinase gene transcripts in the midguts of two tropical insect pests, Scirpophaga incertulas (Wk.) and Helicoverpa armigera (Hb.)

Mazumdar-Leighton, Sudeshna; Babu, C. R.; Bennett, John

doi:10.1016/s0965-1748(99)00097-1

Cited by 40 publications

(33 citation statements)

References 39 publications

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“…The re- Archives of Insect Biochemistry and Physiology mainder possessed a glycine residue in this position. This is an unusual feature for mammalian serine proteases (L. Hedstrom, personal communication) but appears to be common amongst the Lepidoptera (Bown et al, 1997;Zhu et al, 1997;Mazumdar-Leighton et al, 2000) but not other insect orders (Casu et al, 1994;Gaines et al, 1999) or arthropods (Mulenga et al, 2001). Each of the serine proteases contained a conserved Cys 191 residue that forms a disulfide bridge with Cys 220 of loop 2 to stabilize the S1 binding pocket (Wang et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

“…Prior to our study, all other lepidopteran serine proteases examined were found to have a reduced overall lysine content; of special note was the change of Lys 188 , present in mammalian and dipteran trypsins, to Arg 188 (Peterson et al, 1994;Bown et al, 1997;Mazumdar-Leighton et al, 2000). Arginine, with its comparatively higher pKa, would remain protonated under the alkaline conditions of the lepidopteran gut and stabilize the protease active site.…”

Section: May 2003mentioning

confidence: 90%

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Midgut proteases from Mamestra configurata (Lepidoptera: Noctuidae) larvae: Characterization, cDNA cloning, and expressed sequence tag analysis

Hegedus

Baldwin

O’Grady

et al. 2003

Arch Insect Biochem Physiol

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The activities of digestive protease within the midgut of Mamestra configurata (bertha armyworm) larvae were examined using specific substrates and protease inhibitors. The bulk of the activity was associated with serine proteases comprising trypsin-, chymotrypsin-, and elastase-like enzymes. At least 10-15 serine protease isozymes were detected using one-dimension gelatin gel electrophoresis. Cysteine or aspartic protease activities were not present; however, amino- and carboxypeptidase activities were associated with the midgut extract. Midgut proteases were active in the pH range of 5.0-12.0 with peaks at pH 7.5 and 11.0. In general, the middle region of the midgut exhibited a higher pH (approximately 8.0) than either the posterior or anterior regions (approximately 7.3-7.7). Moulting larvae possessed a neutral gut pH that was 0.5-1.5 units below that of feeding larvae. Degenerate PCR and expressed sequence tag (EST)-based approaches were used to isolate 30 distinct serine protease encoding cDNAs from a midgut-specific cDNA library including 8 putative trypsins, 9 chymotrypsins, 1 elastase, and 12 whose potential activities could not be determined. cDNAs encoding three amino- and two carboxypeptidases were also identified. Larvae feeding upon artificial diet containing 0.2% soybean trypsin inhibitor experienced a significant delay in development.

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Section: Discussionmentioning

confidence: 99%

Section: May 2003mentioning

confidence: 90%

Midgut proteases from Mamestra configurata (Lepidoptera: Noctuidae) larvae: Characterization, cDNA cloning, and expressed sequence tag analysis

Hegedus

Baldwin

O’Grady

et al. 2003

Arch Insect Biochem Physiol

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“…Hence, the genes encoding serine and other proteinases of H. armigera have received much attention due to their involvement in the success of overcoming the adverse effects of proteinaceous PIs. Several cDNAs of trypsin, chymotrypsin, elastase and carboxypeptidases have been reported from H. armigera larvae (Bown et al, 1997;Gatehouse et al, 1997;Mazumdar-Leighton et al, 2000;Bown et al, 1998;Bown and Gatehouse, 2004). Gatehouse et al (1997) classified trypsin genes into three subfamilies and chymotrypsin and elastase as individual gene family.…”

Section: Introductionmentioning

confidence: 99%

Gene expression patterns of Helicoverpa armigera gut proteases

Chougule

Giri

Sainani

et al. 2005

Insect Biochemistry and Molecular Biology

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“…Further, presence of at least 28 genes of trypsin-and chymotrypsin-like proteinases in H. armigera with 90% homology and minor differences near the active sites of these proteinases was shown by Bown et al (1997) [26]. Mazumdar-Leighton et al (2000) [36] reported the presence of two transcripts for trypsinlike proteinases in H. armigera. Moderate to high level of chymotrypsin-like activity was detected in the larvae fed on pigeonpea, whereas very low activity was detected in larvae fed on chickpea.…”

Section: Resultsmentioning

confidence: 96%

Protease Inhibitors in Wild Relatives of Pigeonpea against the Cotton Bollworm/Legume Pod Borer, <i>Helicoverpa armigera</i>

Parde¹,

Sharma²,

Kachole³

2012

AJPS

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Cotton bollworm/legume pod borer, Helicoverpa armigera is one of the most damaging pests worldwide. Because of the difficulties associated with chemical control of this pest, emphasis has been placed on developing transgenic plants with resistance to H. armigera. Since toxin genes from the bacterium, Bacillus thuringiensis (Bt) have been deployed on a large scale, there is need to scout for alternate genes which could be deployed alone or in combination with the Bt genes for pest management. Therefore, we evaluated the wild relatives of pigeonpea, which have shown high levels of resistance to this pest, for the protease inhibitors (PIs) under in vivo and in vitro inhibitions. Accessions belonging to Cajanus albicans, C. cajanifolius, C. sericeus, Flemingia bracteata, and Rhynchosia bracteata showed complete inhibition of H. armigera gut proteinases (HaGPs). Some of the C. scarabaeoides accessions (ICPW 116, 152, 278 and 280) exhibited partial inhibition at low concentrations of the PIs. All accessions of wild relatives of pigeonpea showed high to moderate level of inhibition at pH 7.8. Cultivated pigeonpea, ICPL 87 exhibited monomorphism in terms of trypsin inhibitor (TI) and chymotrypsin inhibitor (CTI) isoforms, contrary to the diverse inhibitory profiles of wild pigeonpeas. Cajanus albicans, C. platycarpus, C. scarabaeoides, and R. bracteata showed more number of TI and CTI bands than the cultivated pigeonpea. Protease inhibitor isoforms of wild relatives of pigeonpea showed significant variation in number, band pattern, and protein specificities towards trypsin, chymotrypsin, and H. armigera gut proteinases (HaGPs) as compared to the cultivated pigeonpea. The PIs from the wild relatives of pigeonpea showed considerable potential against the HaGPs, and could be considered as potential candidates for use in genetic transformation of crops for pest management, including H. armigera.

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Identification of novel serine proteinase gene transcripts in the midguts of two tropical insect pests, Scirpophaga incertulas (Wk.) and Helicoverpa armigera (Hb.)

Cited by 40 publications

References 39 publications

Midgut proteases from Mamestra configurata (Lepidoptera: Noctuidae) larvae: Characterization, cDNA cloning, and expressed sequence tag analysis

Midgut proteases from Mamestra configurata (Lepidoptera: Noctuidae) larvae: Characterization, cDNA cloning, and expressed sequence tag analysis

Gene expression patterns of Helicoverpa armigera gut proteases

Protease Inhibitors in Wild Relatives of Pigeonpea against the Cotton Bollworm/Legume Pod Borer, <i>Helicoverpa armigera</i>

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Identification of novel serine proteinase gene transcripts in the midguts of two tropical insect pests, Scirpophaga incertulas (Wk.) and Helicoverpa armigera (Hb.)

Cited by 40 publications

References 39 publications

Midgut proteases from Mamestra configurata (Lepidoptera: Noctuidae) larvae: Characterization, cDNA cloning, and expressed sequence tag analysis

Midgut proteases from Mamestra configurata (Lepidoptera: Noctuidae) larvae: Characterization, cDNA cloning, and expressed sequence tag analysis

Gene expression patterns of Helicoverpa armigera gut proteases

Protease Inhibitors in Wild Relatives of Pigeonpea against the Cotton Bollworm/Legume Pod Borer, &lt;i&gt;Helicoverpa armigera&lt;/i&gt;

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Protease Inhibitors in Wild Relatives of Pigeonpea against the Cotton Bollworm/Legume Pod Borer, <i>Helicoverpa armigera</i>