Complexity in specificities and expression of Helicoverpa armigera gut proteinases explains polyphagous nature of the insect pest
Metadata of CSIR Papers
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| Title |
Complexity in specificities and expression of Helicoverpa armigera gut proteinases explains polyphagous nature of the insect pest
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| Creator |
Patankar, AG
Giri, AP Harsulkar, AM Sainani, MN Deshpande, VV Ranjekar, PK Gupta, VS |
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| Subject |
Biochemistry & Molecular Biology; Entomology
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| Description |
Helicoverpa armigera is a devastating pest of cotton and other important crop plants all over the world. A detailed biochemical investigation of H. armigera gut proteinases is essential for planning effective proteinase inhibitor (PI)-based strategies to counter the insect infestation. In this study, we report the complexity of gut proteinase composition of H, armigera fed on four different host plants, viz. chickpea, pigeonpea, cotton and okra, and during larval development. H. armigera fed on chickpea showed more than 2.5- to 3-fold proteinase activity than those fed on the other host plants. H. armigera gut proteinase composition revealed the predominance of serine proteinase activity; however, the larvae fed on pigeonpea revealed the presence of metalloproteases and low levels of aspartic and cysteine proteases as well. Gut proteinase activity increased during larval development with the highest activity seen in the fifth instar larvae which, however, declined sharply in the sixth instar. Over 90% of the gut proteinase activity of the fifth instar larvae was of the serine proteinase type, however, the second instar larvae showed the presence of proteinases of other mechanistic classes like metalloproteases, aspartic and cysteine proteases along with serine proteinase activity as evident by inhibition studies. Analysis of fecal matter of larvae showed significant increase in proteinase activity when fed on an artificial diet with or without non-host PIs than larvae fed on a natural diet. The diversity in the proteinase activity observed in H. armigera gut and the flexibility in their expression during developmental stages and depending upon the diet provides a base for selection of proper PIs for insect resistance in transgenic crop plants. (C) 2001 Elsevier Science Ltd. All rights reserved.
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| Publisher |
PERGAMON-ELSEVIER SCIENCE LTDOXFORDTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND
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| Date |
2011-09-24T09:04:41Z
2011-09-24T09:04:41Z 2001 |
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| Type |
Article
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| Identifier |
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
0965-1748 http://hdl.handle.net/123456789/24113 |
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| Language |
English
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