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First published online February 9, 2007; 10.1104/pp.107.095588 Plant Physiology 143:1954-1967 (2007) © 2007 American Society of Plant Biologists OPEN ACCESS ARTICLE
Stability of Plant Defense Proteins in the Gut of Insect Herbivores1,[C],[W],[OA]Department of Energy Plant Research Laboratory (H.C., E.G.-V., G.A.H.), Michigan Proteome Consortium (C.G.W.), and Department of Biochemistry and Molecular Biology (G.A.H.), Michigan State University, East Lansing, Michigan 48824
Plant defense against insect herbivores is mediated in part by enzymes that impair digestive processes in the insect gut. Little is known about the evolutionary origins of these enzymes, their distribution in the plant kingdom, or the mechanisms by which they act in the protease-rich environment of the animal digestive tract. One example of such an enzyme is threonine (Thr) deaminase (TD), which in tomato (Solanum lycopersicum) serves a dual role in isoleucine (Ile) biosynthesis in planta and Thr degradation in the insect midgut. Here, we report that tomato uses different TD isozymes to perform these functions. Whereas the constitutively expressed TD1 has a housekeeping role in Ile biosynthesis, expression of TD2 in leaves is activated by the jasmonate signaling pathway in response to herbivore attack. Ingestion of tomato foliage by specialist (Manduca sexta) and generalist (Trichoplusia ni) insect herbivores triggered proteolytic removal of TD2's C-terminal regulatory domain, resulting in an enzyme that degrades Thr without being inhibited through feedback by Ile. This processed form (pTD2) of TD2 accumulated to high levels in the insect midgut and feces (frass). Purified pTD2 exhibited biochemical properties that are consistent with a postingestive role in defense. Shotgun proteomic analysis of frass from tomato-reared M. sexta identified pTD2 as one of the most abundant proteins in the excrement. Among the other tomato proteins identified were several jasmonate-inducible proteins that have a known or proposed role in anti-insect defense. Subtilisin-like proteases and other pathogenesis-related proteins, as well as proteins of unknown function, were also cataloged. We conclude that proteomic analysis of frass from insect herbivores provides a robust experimental approach to identify hyperstable plant proteins that serve important roles in defense.
1 This work was supported by the U.S. Department of Agriculture (grant no. 2007–35604–17791) and by the U.S. Department of Energy (grant no. DE–FG02–91ER20021 to G.A.H.). 2 These authors contributed equally to the paper. 3 Present address: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164. The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Gregg A. Howe (howeg{at}msu.edu). [C] Some figures in this article are displayed in color online but in black and white in the print edition. [W] The online version of this article contains Web-only data. [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.107.095588 * Corresponding author; e-mail howeg{at}msu.edu; fax 517–353–9168. Received January 6, 2007; accepted January 29, 2007; published February 9, 2007. This article has been cited by other articles:
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