Title: | ATP hydrolyzing salivary enzymes of caterpillars suppress plant defenses |
Author(s): | Wu S; Peiffer M; Luthe DS; Felton GW; |
Address: | "Department of Entomology and Center for Chemical Ecology, Pennsylvania State University, University Park, Pennsylvania, United States of America" |
DOI: | 10.1371/journal.pone.0041947 |
ISSN/ISBN: | 1932-6203 (Electronic) 1932-6203 (Linking) |
Abstract: | "The oral secretions of herbivores are important recognition cues that can be used by plants to mediate induced defenses. In this study, a degradation of adenosine-5'-triphosphate (ATP) in tomato leaves was detected after treatment with Helicoverpa zea saliva. Correspondingly, a high level of ATPase activity in saliva was detected and three ATP hydrolyzing enzymes: apyrase, ATP synthase and ATPase 13A1 were identified in salivary glands. To determine the functions of these proteins in mediating defenses, they were cloned from H. zea and expressed in Escherichia coli. By applying the purified expressed apyrase, ATP synthase or ATPase 13A1 to wounded tomato leaves, it was determined that these ATP hydrolyzing enzymes suppressed the defensive genes regulated by the jasmonic acid and ethylene pathways in tomato plant. Suppression of glandular trichome production was also observed after treatment. Blood-feeding arthropods employ 5'-nucleotidase family of apyrases to circumvent host responses and the H. zea apyrase, is also a member of this family. The comparatively high degree of sequence similarity of the H. zea salivary apyrase with mosquito apyrases suggests a broader evolutionary role for salivary apyrases than previously envisioned" |
Keywords: | "Adenosine Triphosphate/*metabolism Animals Gene Expression Regulation, Enzymologic Hydrolysis Lepidoptera/*enzymology/genetics/physiology Solanum lycopersicum/*immunology/*metabolism/parasitology Plant Leaves/metabolism Saliva/*enzymology Sequence Analysi;" |
Notes: | "MedlineWu, Shuang Peiffer, Michelle Luthe, Dawn S Felton, Gary W eng Research Support, U.S. Gov't, Non-P.H.S. 2012/08/01 PLoS One. 2012; 7(7):e41947. doi: 10.1371/journal.pone.0041947. Epub 2012 Jul 25" |