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Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania
Vip3A proteins are important for the control of spodopteran pests in crops, including Spodoptera frugiperda (fall armyworm). Native Vip3Ab1 controls S. frugiperda, but it is ineffective against S. eridania (southern armyworm), a major pest of soybean in South America. Recently, a Vip3Ab1 chimera wit...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6563307/ https://www.ncbi.nlm.nih.gov/pubmed/31100873 http://dx.doi.org/10.3390/toxins11050276 |
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author | Bowling, Andrew J. Sopko, Megan S. Tan, Sek Yee Larsen, Cory M. Pence, Heather E. Zack, Marc D. |
author_facet | Bowling, Andrew J. Sopko, Megan S. Tan, Sek Yee Larsen, Cory M. Pence, Heather E. Zack, Marc D. |
author_sort | Bowling, Andrew J. |
collection | PubMed |
description | Vip3A proteins are important for the control of spodopteran pests in crops, including Spodoptera frugiperda (fall armyworm). Native Vip3Ab1 controls S. frugiperda, but it is ineffective against S. eridania (southern armyworm), a major pest of soybean in South America. Recently, a Vip3Ab1 chimera with a modified C-terminus was described, Vip3Ab1-740, which has increased potency against S. eridania while maintaining activity against S. frugiperda. As S. frugiperda and S. eridania are differentially susceptible to Vip3Ab1, experiments were conducted to identify and understand the mechanism by which this expanded potency is conferred. The role of protein stability, processing, and in vivo effects of Vip3Ab1 and Vip3Ab1-740 in both of these species was investigated. Biochemical characterization of the midgut fluids of these two species indicated no obvious differences in the composition and activity of digestive enzymes, which protease inhibitor studies indicated were likely serine proteases. Histological examination demonstrated that both proteins cause midgut disruption in S. frugiperda, while only Vip3Ab1-740 affects S. eridania. Immunolocalization indicated that both proteins were present in the midgut of S. frugiperda, but only Vip3Ab1-740 was detected in the midgut of S. eridania. We conclude that the gain of toxicity of Vip3Ab1-740 to S. eridania is due to an increase in protein stability in the midgut, which was conferred by C-terminal modification. |
format | Online Article Text |
id | pubmed-6563307 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-65633072019-06-17 Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania Bowling, Andrew J. Sopko, Megan S. Tan, Sek Yee Larsen, Cory M. Pence, Heather E. Zack, Marc D. Toxins (Basel) Article Vip3A proteins are important for the control of spodopteran pests in crops, including Spodoptera frugiperda (fall armyworm). Native Vip3Ab1 controls S. frugiperda, but it is ineffective against S. eridania (southern armyworm), a major pest of soybean in South America. Recently, a Vip3Ab1 chimera with a modified C-terminus was described, Vip3Ab1-740, which has increased potency against S. eridania while maintaining activity against S. frugiperda. As S. frugiperda and S. eridania are differentially susceptible to Vip3Ab1, experiments were conducted to identify and understand the mechanism by which this expanded potency is conferred. The role of protein stability, processing, and in vivo effects of Vip3Ab1 and Vip3Ab1-740 in both of these species was investigated. Biochemical characterization of the midgut fluids of these two species indicated no obvious differences in the composition and activity of digestive enzymes, which protease inhibitor studies indicated were likely serine proteases. Histological examination demonstrated that both proteins cause midgut disruption in S. frugiperda, while only Vip3Ab1-740 affects S. eridania. Immunolocalization indicated that both proteins were present in the midgut of S. frugiperda, but only Vip3Ab1-740 was detected in the midgut of S. eridania. We conclude that the gain of toxicity of Vip3Ab1-740 to S. eridania is due to an increase in protein stability in the midgut, which was conferred by C-terminal modification. MDPI 2019-05-16 /pmc/articles/PMC6563307/ /pubmed/31100873 http://dx.doi.org/10.3390/toxins11050276 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bowling, Andrew J. Sopko, Megan S. Tan, Sek Yee Larsen, Cory M. Pence, Heather E. Zack, Marc D. Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania |
title | Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania |
title_full | Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania |
title_fullStr | Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania |
title_full_unstemmed | Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania |
title_short | Insecticidal Activity of a Vip3Ab1 Chimera Is Conferred by Improved Protein Stability in the Midgut of Spodoptera eridania |
title_sort | insecticidal activity of a vip3ab1 chimera is conferred by improved protein stability in the midgut of spodoptera eridania |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6563307/ https://www.ncbi.nlm.nih.gov/pubmed/31100873 http://dx.doi.org/10.3390/toxins11050276 |
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