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Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene
Proteinase inhibitors provide a means of engineering plant resistance to insect pests. A Beta vulgaris serine proteinase inhibitor gene (BvSTI) was fused to the constitutive CaMV35S promoter for over-expression in Nicotiana benthamiana plants to study its effect on lepidopteran insect pests. Indepen...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3582505/ https://www.ncbi.nlm.nih.gov/pubmed/23468963 http://dx.doi.org/10.1371/journal.pone.0057303 |
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author | Smigocki, Ann C. Ivic-Haymes, Snezana Li, Haiyan Savić, Jelena |
author_facet | Smigocki, Ann C. Ivic-Haymes, Snezana Li, Haiyan Savić, Jelena |
author_sort | Smigocki, Ann C. |
collection | PubMed |
description | Proteinase inhibitors provide a means of engineering plant resistance to insect pests. A Beta vulgaris serine proteinase inhibitor gene (BvSTI) was fused to the constitutive CaMV35S promoter for over-expression in Nicotiana benthamiana plants to study its effect on lepidopteran insect pests. Independently derived BvSTI transgenic tobacco T2 homozygous progeny were shown to have relatively high BvSTI gene transcript levels. BvSTI-specific polyclonal antibodies cross-reacted with the expected 30 kDA recombinant BvSTI protein on Western blots. In gel trypsin inhibitor activity assays revealed a major clear zone that corresponded to the BvSTI proteinase inhibitor that was not detected in the untransformed control plants. BvSTI-transgenic plants were bioassayed for resistance to five lepidopteran insect pests. Spodoptera frugiperda, S. exigua and Manduca sexta larvae fed BvSTI leaves had significant reductions in larval weights as compared to larvae fed on untransformed leaves. In contrast, larval weights increased relative to the controls when Heliothis virescens and Agrotis ipsilon larvae were fed on BvSTI leaves. As the larvae entered the pupal stage, pupal sizes reflected the overall larval weights. Some developmental abnormalities of the pupae and emerging moths were noted. These findings suggest that the sugar beet BvSTI gene may prove useful for effective control of several different lepidopteran insect pests in genetically modified tobacco and other plants. The sugar beet serine proteinase inhibitor may be more effective for insect control because sugar beet is cropped in restricted geographical areas thus limiting the exposure of the insects to sugar beet proteinase inhibitors and build up of non-sensitive midgut proteases. |
format | Online Article Text |
id | pubmed-3582505 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-35825052013-03-06 Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene Smigocki, Ann C. Ivic-Haymes, Snezana Li, Haiyan Savić, Jelena PLoS One Research Article Proteinase inhibitors provide a means of engineering plant resistance to insect pests. A Beta vulgaris serine proteinase inhibitor gene (BvSTI) was fused to the constitutive CaMV35S promoter for over-expression in Nicotiana benthamiana plants to study its effect on lepidopteran insect pests. Independently derived BvSTI transgenic tobacco T2 homozygous progeny were shown to have relatively high BvSTI gene transcript levels. BvSTI-specific polyclonal antibodies cross-reacted with the expected 30 kDA recombinant BvSTI protein on Western blots. In gel trypsin inhibitor activity assays revealed a major clear zone that corresponded to the BvSTI proteinase inhibitor that was not detected in the untransformed control plants. BvSTI-transgenic plants were bioassayed for resistance to five lepidopteran insect pests. Spodoptera frugiperda, S. exigua and Manduca sexta larvae fed BvSTI leaves had significant reductions in larval weights as compared to larvae fed on untransformed leaves. In contrast, larval weights increased relative to the controls when Heliothis virescens and Agrotis ipsilon larvae were fed on BvSTI leaves. As the larvae entered the pupal stage, pupal sizes reflected the overall larval weights. Some developmental abnormalities of the pupae and emerging moths were noted. These findings suggest that the sugar beet BvSTI gene may prove useful for effective control of several different lepidopteran insect pests in genetically modified tobacco and other plants. The sugar beet serine proteinase inhibitor may be more effective for insect control because sugar beet is cropped in restricted geographical areas thus limiting the exposure of the insects to sugar beet proteinase inhibitors and build up of non-sensitive midgut proteases. Public Library of Science 2013-02-26 /pmc/articles/PMC3582505/ /pubmed/23468963 http://dx.doi.org/10.1371/journal.pone.0057303 Text en https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. |
spellingShingle | Research Article Smigocki, Ann C. Ivic-Haymes, Snezana Li, Haiyan Savić, Jelena Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene |
title | Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene |
title_full | Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene |
title_fullStr | Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene |
title_full_unstemmed | Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene |
title_short | Pest Protection Conferred by a Beta vulgaris Serine Proteinase Inhibitor Gene |
title_sort | pest protection conferred by a beta vulgaris serine proteinase inhibitor gene |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3582505/ https://www.ncbi.nlm.nih.gov/pubmed/23468963 http://dx.doi.org/10.1371/journal.pone.0057303 |
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