Complexity in specificities and expression of Helicoverpa armigera gut proteinases explains polyphagous nature of the insect pest

Patankar, Aparna G.; Giri, Ashok P.; Harsulkar, Abhay; Sainani, Mohini N.; Deshpande, Vasanti; Ranjekar, P. K.; Gupta, Vidya S.

doi:10.1016/s0965-1748(00)00150-8

Cited by 170 publications

(127 citation statements)

References 43 publications

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“…Serine proteases are known to dominate the larval gut environment and contribute to about 95% of the total digestive activity. Beneath the complexity of multiple protease specificities, there usually exists an array of diverse protease isoforms; for example, the gut of Helicoverpa armigera alone is known to contain about twenty different types of active serine protease isoforms at any given moment [1][2][3]. This multitude of isoforms does seem unnecessary, especially when only a few of them (e.g., trypsins) contribute significantly to digestion.…”

Section: Multiple Protease Specificities and Isoforms In Lepidopteramentioning

confidence: 99%

Structural and functional diversities in lepidopteran serine proteases

Srinivasan

Giri

Gupta

2006

Cellular and Molecular Biology Letters

211

164

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Primary protein-digestion in Lepidopteran larvae relies on serine proteases like trypsin and chymotrypsin. Efforts toward the classification and characterization of digestive proteases have unraveled a considerable diversity in the specificity and mechanistic classes of gut proteases. Though the evolutionary significance of mutations that lead to structural diversity in serine proteases has been well characterized, detailing the resultant functional diversity has continually posed a challenge to researchers. Functional diversity can be correlated to the adaptation of insects to various host-plants as well as to exposure of insects to naturally occurring antagonistic biomolecules such as plant-derived protease inhibitors (PIs) and lectins. Current research is focused on deciphering the changes in protease specificities and activities arising from altered amino acids at the active site, specificity-determining pockets and other regions, which influence activity. Some insight has been gained through in silico modeling and simulation experiments, aided by the limited availability of characterized proteases. We examine the structurally and functionally diverse Lepidopteran serine proteases, and assess their influence on larval digestive processes and on overall insect physiology.

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Section: Multiple Protease Specificities and Isoforms In Lepidopteramentioning

confidence: 99%

Structural and functional diversities in lepidopteran serine proteases

Srinivasan

Giri

Gupta

2006

Cellular and Molecular Biology Letters

211

164

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“…The data resulting from zymogram studies clearly revealed that PMSF and TLCK reduced the intensity of bands compared to the control in the gel electrophoresis zymogram. Also, in the case of lepidopteran species, trypsin, chymotrypsin, elastase-like proteinases, aminopeptidases and carboxypeptidases comprise the gut proteolytic profiles dominantly (Terra & Ferreira 1994) and lepidopteran larvae use serine protease for protein digestion (Patankar et al 2001;Josephrajkumar et al 2006;Chougule et al 2008). In contrast, Nakonieczny et al (2007) showed a minor role of trypsin and chymotrypsin in protein digestion in Apollo butterfly, Parnassius apollo ssp.…”

Section: Discussionmentioning

confidence: 99%

“…These inhibitors can bind with dominant digestive proteases of insects feeding on the host plants, impairing their digestion and retarding growth and larval development in some insect species including lepidoptera (Gatehouse et al 2000). Serine proteases and metallo-exopeptidase are dominant active proteases in the digestive system of lepidopteran larvae (Patankar et al 2001;Josephrajkumar et al 2006;Chougule et al 2008). Also, serine proteases have been reported from the digestive tracts of many insects belong to different orders and families and these enzymes are inhibited by serine protease inhibitors available in legume and cereal plants.…”

mentioning

confidence: 99%

“…Their use in the insect control is notable based on several studies indicating their effectiveness in disruption of protease digestion. The lepidopteran larvae use a complex proteolytic enzymes including trypsins, chymotrypsins, elastases, cathepsin-B like proteases, aminopeptidases, and carboxypeptidases for protein digestion and many serine proteases are dominant in the larval gut (Patankar et al 2001;Srinivasan et al 2006;Chougule et al 2008;Tabatabaei et al 2011). Insect digestive proteases have different biochemical properties.…”

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confidence: 99%

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Identification and characterisation of gut proteases in the fig tree skeletoniser moth, Choreutis nemorana Hübner (Lepidoptera: Choreutidae)

Chitgar¹,

Ghadamyari²,

Sharifi³

2013

Plant Prot. Sci.

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The biochemical properties of proteases from the digestive system of the fig tree skeletonizer moth, Choreutis nemorana, were determined. Gut extracts of C. nemorana larvae were analysed using different specific peptide substrates and proteinase inhibitors. The optimal pH and temperature for proteolytic activities using azocasein as substrate were obtained as pH 11 and 45°C, respectively. In the case of N-benzoyl-l-arg-p-nitroanilide as substrate, the enzyme showed the maximum tryptic activity at pH 11. The kinetic parameters of trypsin-like proteases indicated that the K m and V max values of trypsin in the gut of C. nemorana were 0.157 ± 0.006mM and 0.188 ± 0.005 µmol/min/mg protein. Using specific proteolytic inhibitors, the inhibitors including phenyl methane sulfonyl fluoride, N-p-tosyl-l-lys chloromethyl ketone and ethylene diamine tetraacetic acid showed the greatest inhibitory effect on total proteolytic activity. These results indicated that serine proteinases accounted for the major proteases in the gut of C. nemorana. Inhibition assays and zymogram analysis showed that only small amounts of cysteine proteases are present in the digestive system of C. nemorana.

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“…For example, insects can detoxify allelochemicals via the inducible cytochrome P450 monoxygenase system (Berenbaum, 1991;Berenbaum et al, 1992;Rose et al, 1992;Hung et al, 1995;Scott et al, 1998;Harrison et al, 2001;Li et al, 2002), or produce or upregulate alternative proteases that are not susceptible to inhibition, or that can digest the proteinase inhibitors present in the diet (Broadway, 1996(Broadway, , 1997Wu et al, 1997;Patankar et al, 1999Patankar et al, , 2001Moon et al, 2004).…”

Section: Nsmentioning

confidence: 99%

Quantitative genetics of preference and performance on chickpeas in the noctuid moth, Helicoverpa armigera

Cotter

Edwards

2006

Heredity

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If a novel, resistant host-plant genotype arises in the environment, insect populations utilising that host must be able to overcome that resistance in order that they can maintain their ability to feed on that host. The ability to evolve resistance to host-plant defences depends upon additive genetic variation in larval performance and adult host-choice preference. To investigate the potential of a generalist herbivore to respond to a novel resistant host, we estimated the heritability of larval performance in the noctuid moth, Helicoverpa armigera, on a resistant and a susceptible variety of the chickpea, Cicer arietinum, at two different life stages. Heritability estimates were higher for neonates than for third-instar larvae, suggesting that their ability to establish on plants could be key to the evolution of resistance in this species; however, further information regarding the nature of selection in the field would be required to confirm this prediction. There was no genetic correlation between larval performance and oviposition preference, indicating that female moths do not choose the most suitable plant for their offspring. We also found significant genotype by environment interactions for neonates (but not third-instar larvae), suggesting that the larval response to different plant genotypes is stage-specific in this species.

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Complexity in specificities and expression of Helicoverpa armigera gut proteinases explains polyphagous nature of the insect pest

Cited by 170 publications

References 43 publications

Structural and functional diversities in lepidopteran serine proteases

Structural and functional diversities in lepidopteran serine proteases

Identification and characterisation of gut proteases in the fig tree skeletoniser moth, Choreutis nemorana Hübner (Lepidoptera: Choreutidae)

Quantitative genetics of preference and performance on chickpeas in the noctuid moth, Helicoverpa armigera

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