First published online October 28, 2005; 10.1104/pp.105.066837
Plant Physiology 139:1545-1556 (2005)
© 2005 American Society of Plant Biologists
PLANTS INTERACTING WITH OTHER ORGANISMS
Arabidopsis Vegetative Storage Protein Is an Anti-Insect Acid Phosphatase
Yilin Liu,
Ji-Eun Ahn,
Sumana Datta,
Ron A. Salzman,
Jaewoong Moon,
Beatrice Huyghues-Despointes,
Barry Pittendrigh,
Larry L. Murdock,
Hisashi Koiwa and
Keyan Zhu-Salzman*
Department of Entomology (Y.L., J.-E.A., R.A.S., J.M., K.Z.-S.), Department of Biochemistry and Biophysics (S.D.), Department of Medical Biochemistry and Genetics (B.H.-D.), and Department of Horticultural Sciences (H.K.), Texas A&M University, College Station, Texas 77843; and Department of Entomology, Purdue University, West Lafayette, Indiana 47907 (B.P., L.L.M.)
Indirect evidence previously suggested that Arabidopsis (Arabidopsis thaliana) vegetative storage protein (VSP) could play a role in defense against herbivorous insects. To test this hypothesis, other AtVSP-like sequences in Arabidopsis were identified through a Basic Local Alignment Search Tool search, and their transcriptional profiles were investigated. In response to methyl jasmonate application or phosphate starvation, AtVSP and AtVSP-like genes exhibited differential expression patterns, suggesting distinct roles played by each member. Arabidopsis VSP2 (AtVSP2), a gene induced by wounding, methyl jasmonate, insect feeding, and phosphate deprivation, was selected for bacterial expression and functional characterization. The recombinant protein exhibited a divalent cation-dependent phosphatase activity in the acid pH range. When incorporated into the diets of three coleopteran and dipteran insects that have acidic gut lumen, recombinant AtVSP2 significantly delayed development of the insects and increased their mortality. To further determine the biochemical basis of the anti-insect activity of the protein, the nucleophilic aspartic acid-119 residue at the conserved DXDXT signature motif was substituted by glutamic acid via site-directed mutagenesis. This single-amino acid alteration did not compromise the protein's secondary or tertiary structure, but resulted in complete loss of its acid phosphatase activity as well as its anti-insect activity. Collectively, we conclude that AtVSP2 is an anti-insect protein and that its defense function is correlated with its acid phosphatase activity.
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: Keyan Zhu-Salzman (ksalzman{at}tamu.edu).
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.066837.
* Corresponding author; e-mail ksalzman{at}tamu.edu; fax 979–862–4790.
Received June 9, 2005;
returned for revision July 25, 2005;
accepted August 18, 2005.
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