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ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses
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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3405022/ https://www.ncbi.nlm.nih.gov/pubmed/22848670 http://dx.doi.org/10.1371/journal.pone.0041947 |
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author | Wu, Shuang Peiffer, Michelle Luthe, Dawn S. Felton, Gary W. |
author_facet | Wu, Shuang Peiffer, Michelle Luthe, Dawn S. Felton, Gary W. |
author_sort | Wu, Shuang |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-3405022 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34050222012-07-30 ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses Wu, Shuang Peiffer, Michelle Luthe, Dawn S. Felton, Gary W. PLoS One Research Article 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. Public Library of Science 2012-07-25 /pmc/articles/PMC3405022/ /pubmed/22848670 http://dx.doi.org/10.1371/journal.pone.0041947 Text en Wu et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Wu, Shuang Peiffer, Michelle Luthe, Dawn S. Felton, Gary W. ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses |
title | ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses |
title_full | ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses |
title_fullStr | ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses |
title_full_unstemmed | ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses |
title_short | ATP Hydrolyzing Salivary Enzymes of Caterpillars Suppress Plant Defenses |
title_sort | atp hydrolyzing salivary enzymes of caterpillars suppress plant defenses |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3405022/ https://www.ncbi.nlm.nih.gov/pubmed/22848670 http://dx.doi.org/10.1371/journal.pone.0041947 |
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