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New Insights into the Plutella xylostella Detoxifying Enzymes: Sequence Evolution, Structural Similarity, Functional Diversity, and Application Prospects of Glucosinolate Sulfatases
[Image: see text] Brassica plants have glucosinolate (GLs)-myrosinase defense mechanisms to deter herbivores. However, Plutella xylostella specifically feeds on Brassica vegetables. The larvae possess three glucosinolate sulfatases (PxGSS1–3) that compete with plant myrosinase for shared GLs substra...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10375594/ https://www.ncbi.nlm.nih.gov/pubmed/37462091 http://dx.doi.org/10.1021/acs.jafc.3c03246 |
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author | Chen, Wei Amir, Muhammad Bilal Liao, Yuan Yu, Haizhong He, Weiyi Lu, Zhanjun |
author_facet | Chen, Wei Amir, Muhammad Bilal Liao, Yuan Yu, Haizhong He, Weiyi Lu, Zhanjun |
author_sort | Chen, Wei |
collection | PubMed |
description | [Image: see text] Brassica plants have glucosinolate (GLs)-myrosinase defense mechanisms to deter herbivores. However, Plutella xylostella specifically feeds on Brassica vegetables. The larvae possess three glucosinolate sulfatases (PxGSS1–3) that compete with plant myrosinase for shared GLs substrates and produce nontoxic desulfo-GLs (deGLs). Although PxGSSs are considered potential targets for pest control, the lack of a comprehensive review has hindered the development of PxGSSs-targeted pest control methods. Recent advances in integrative multi-omics analysis, substrate-enzyme kinetics, and molecular biological techniques have elucidated the evolutionary origin and functional diversity of these three PxGSSs. This review summarizes research progress on PxGSSs over the past 20 years, covering sequence properties, evolution, protein modification, enzyme activity, structural variation, substrate specificity, and interaction scenarios based on functional diversity. Finally, we discussed the potential applications of PxGSSs-targeted pest control technologies driven by artificial intelligence, including CRISPR/Cas9-mediated gene drive, transgenic plant-mediated RNAi, small-molecule inhibitors, and peptide inhibitors. These technologies have the potential to overcome current management challenges and promote the development and field application of PxGSSs-targeted pest control. |
format | Online Article Text |
id | pubmed-10375594 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-103755942023-07-29 New Insights into the Plutella xylostella Detoxifying Enzymes: Sequence Evolution, Structural Similarity, Functional Diversity, and Application Prospects of Glucosinolate Sulfatases Chen, Wei Amir, Muhammad Bilal Liao, Yuan Yu, Haizhong He, Weiyi Lu, Zhanjun J Agric Food Chem [Image: see text] Brassica plants have glucosinolate (GLs)-myrosinase defense mechanisms to deter herbivores. However, Plutella xylostella specifically feeds on Brassica vegetables. The larvae possess three glucosinolate sulfatases (PxGSS1–3) that compete with plant myrosinase for shared GLs substrates and produce nontoxic desulfo-GLs (deGLs). Although PxGSSs are considered potential targets for pest control, the lack of a comprehensive review has hindered the development of PxGSSs-targeted pest control methods. Recent advances in integrative multi-omics analysis, substrate-enzyme kinetics, and molecular biological techniques have elucidated the evolutionary origin and functional diversity of these three PxGSSs. This review summarizes research progress on PxGSSs over the past 20 years, covering sequence properties, evolution, protein modification, enzyme activity, structural variation, substrate specificity, and interaction scenarios based on functional diversity. Finally, we discussed the potential applications of PxGSSs-targeted pest control technologies driven by artificial intelligence, including CRISPR/Cas9-mediated gene drive, transgenic plant-mediated RNAi, small-molecule inhibitors, and peptide inhibitors. These technologies have the potential to overcome current management challenges and promote the development and field application of PxGSSs-targeted pest control. American Chemical Society 2023-07-18 /pmc/articles/PMC10375594/ /pubmed/37462091 http://dx.doi.org/10.1021/acs.jafc.3c03246 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Chen, Wei Amir, Muhammad Bilal Liao, Yuan Yu, Haizhong He, Weiyi Lu, Zhanjun New Insights into the Plutella xylostella Detoxifying Enzymes: Sequence Evolution, Structural Similarity, Functional Diversity, and Application Prospects of Glucosinolate Sulfatases |
title | New Insights into
the Plutella xylostella Detoxifying Enzymes: Sequence
Evolution, Structural Similarity,
Functional Diversity, and Application Prospects of Glucosinolate Sulfatases |
title_full | New Insights into
the Plutella xylostella Detoxifying Enzymes: Sequence
Evolution, Structural Similarity,
Functional Diversity, and Application Prospects of Glucosinolate Sulfatases |
title_fullStr | New Insights into
the Plutella xylostella Detoxifying Enzymes: Sequence
Evolution, Structural Similarity,
Functional Diversity, and Application Prospects of Glucosinolate Sulfatases |
title_full_unstemmed | New Insights into
the Plutella xylostella Detoxifying Enzymes: Sequence
Evolution, Structural Similarity,
Functional Diversity, and Application Prospects of Glucosinolate Sulfatases |
title_short | New Insights into
the Plutella xylostella Detoxifying Enzymes: Sequence
Evolution, Structural Similarity,
Functional Diversity, and Application Prospects of Glucosinolate Sulfatases |
title_sort | new insights into
the plutella xylostella detoxifying enzymes: sequence
evolution, structural similarity,
functional diversity, and application prospects of glucosinolate sulfatases |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10375594/ https://www.ncbi.nlm.nih.gov/pubmed/37462091 http://dx.doi.org/10.1021/acs.jafc.3c03246 |
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