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Chapter category: Agricultural Biotechnology

Control of Phytophagous Insect Pests Using Serine Proteinase Inhibitors

This chapter appears in the following book:

Recombinant Protease Inhibitors in Plants

Edited by: Dominique Michaud
ISBN: 1-58706-007-8
» Get more information about this book at landesbioscience.com «

Chapter authors:
John A. Gatehouse, Angharad M.R. Gatehouse and David P. Bown

The role of proteinase inhibitors (PIs) in plant defense against predators and pathogens is now well established. Although diverse endogenous functions for these proteins have been proposed, ranging from regulators of endogenous proteinases to storage proteins, evidence for many of the roles is partial, or confined to isolated examples. On the other hand, many PIs have been shown to act as defensive compounds by direct assay or by expression in transgenic plants, and a body of evidence consistent with their role in plant defense has been accumulated. The case for serine PIs as defensive compounds against predators is particularly clearcut, since the major proteinases present in plants, used for processes such as protein mobilization in storage tissues, contain a cysteine residue as the catalytically active nucleophile in the enzyme active site. Serine proteinases are apparently not used by plants in processes involving largescale protein digestion, and thus the presence of significant quantities of inhibitors with specificity towards these enzymes in plants cannot be for the purposes of regulating endogenous proteinase activity. In contrast, a major role for serine PIs in animals seems to be to block the activity of endogenous proteinases in tissues where this activity would be harmful, as is the case with the pancreatic trypsin inhibitors found in mammals. The presence of significant amounts of serine PIs in plant tissues therefore suggests not an endogenous role, either protective or regulatory, but instead suggests that the targets of these inhibitors are the digestive proteinases of phytophagous animals.

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