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Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests

In this work, we characterized 2 novel insecticidal proteins; Vip3Ab1 and Vip3Bc1. These proteins display unique insecticidal spectra and have differential rates of processing by lepidopteran digestive enzymes. Furthermore, we have found that both proteins exist as tetramers in their native state be...

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Autores principales: Zack, Marc D., Sopko, Megan S., Frey, Meghan L., Wang, Xiujuan, Tan, Sek Yee, Arruda, Jennifer M., Letherer, Ted T., Narva, Kenneth E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593919/
https://www.ncbi.nlm.nih.gov/pubmed/28894249
http://dx.doi.org/10.1038/s41598-017-11702-2
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author Zack, Marc D.
Sopko, Megan S.
Frey, Meghan L.
Wang, Xiujuan
Tan, Sek Yee
Arruda, Jennifer M.
Letherer, Ted T.
Narva, Kenneth E.
author_facet Zack, Marc D.
Sopko, Megan S.
Frey, Meghan L.
Wang, Xiujuan
Tan, Sek Yee
Arruda, Jennifer M.
Letherer, Ted T.
Narva, Kenneth E.
author_sort Zack, Marc D.
collection PubMed
description In this work, we characterized 2 novel insecticidal proteins; Vip3Ab1 and Vip3Bc1. These proteins display unique insecticidal spectra and have differential rates of processing by lepidopteran digestive enzymes. Furthermore, we have found that both proteins exist as tetramers in their native state before and after proteolysis. In addition, we expressed truncated forms and protein chimeras to gain a deeper understanding of toxin specificity and stability. Our study confirms a role for the C-terminal 65 kDa domain in directing insect specificity. Importantly, these data also indicate a specific interaction between the 20 kDa amino terminus and 65 kDa carboxy terminus, after proteolytic processing. We demonstrate the C-terminal 65 kDa to be labile in native proteolytic conditions in absence of the 20 kDa N-terminus. Thus, the 20 kDa fragment functions to provide stability to the C-terminal domain, which is necessary for lethal toxicity against lepidopteran insects.
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spelling pubmed-55939192017-09-13 Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests Zack, Marc D. Sopko, Megan S. Frey, Meghan L. Wang, Xiujuan Tan, Sek Yee Arruda, Jennifer M. Letherer, Ted T. Narva, Kenneth E. Sci Rep Article In this work, we characterized 2 novel insecticidal proteins; Vip3Ab1 and Vip3Bc1. These proteins display unique insecticidal spectra and have differential rates of processing by lepidopteran digestive enzymes. Furthermore, we have found that both proteins exist as tetramers in their native state before and after proteolysis. In addition, we expressed truncated forms and protein chimeras to gain a deeper understanding of toxin specificity and stability. Our study confirms a role for the C-terminal 65 kDa domain in directing insect specificity. Importantly, these data also indicate a specific interaction between the 20 kDa amino terminus and 65 kDa carboxy terminus, after proteolytic processing. We demonstrate the C-terminal 65 kDa to be labile in native proteolytic conditions in absence of the 20 kDa N-terminus. Thus, the 20 kDa fragment functions to provide stability to the C-terminal domain, which is necessary for lethal toxicity against lepidopteran insects. Nature Publishing Group UK 2017-09-11 /pmc/articles/PMC5593919/ /pubmed/28894249 http://dx.doi.org/10.1038/s41598-017-11702-2 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Zack, Marc D.
Sopko, Megan S.
Frey, Meghan L.
Wang, Xiujuan
Tan, Sek Yee
Arruda, Jennifer M.
Letherer, Ted T.
Narva, Kenneth E.
Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests
title Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests
title_full Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests
title_fullStr Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests
title_full_unstemmed Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests
title_short Functional characterization of Vip3Ab1 and Vip3Bc1: Two novel insecticidal proteins with differential activity against lepidopteran pests
title_sort functional characterization of vip3ab1 and vip3bc1: two novel insecticidal proteins with differential activity against lepidopteran pests
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593919/
https://www.ncbi.nlm.nih.gov/pubmed/28894249
http://dx.doi.org/10.1038/s41598-017-11702-2
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