A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite

Gut enzymes can metabolize plant defense compounds and thereby affect the growth and fitness of insect herbivores. Whether these enzymes also influence feeding preference is largely unknown. We studied the metabolization of taraxinic acid β-D-glucopyranosyl ester (TA-G), a sesquiterpene lactone of t...

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Autores principales: Meret Huber, Thomas Roder, Sandra Irmisch, Alexander Riedel, Saskia Gablenz, Julia Fricke, Peter Rahfeld, Michael Reichelt, Christian Paetz, Nicole Liechti, Lingfei Hu, Zoe Bont, Ye Meng, Wei Huang, Christelle AM Robert, Jonathan Gershenzon, Matthias Erb
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spelling oai:doaj.org-article:a447ed9d0bc24028bd2ac0f7ba6576702021-11-25T12:33:45ZA beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite10.7554/eLife.686422050-084Xe68642https://doaj.org/article/a447ed9d0bc24028bd2ac0f7ba6576702021-10-01T00:00:00Zhttps://elifesciences.org/articles/68642https://doaj.org/toc/2050-084XGut enzymes can metabolize plant defense compounds and thereby affect the growth and fitness of insect herbivores. Whether these enzymes also influence feeding preference is largely unknown. We studied the metabolization of taraxinic acid β-D-glucopyranosyl ester (TA-G), a sesquiterpene lactone of the common dandelion (Taraxacum officinale) that deters its major root herbivore, the common cockchafer larva (Melolontha melolontha). We have demonstrated that TA-G is rapidly deglucosylated and conjugated to glutathione in the insect gut. A broad-spectrum M. melolontha β-glucosidase, Mm_bGlc17, is sufficient and necessary for TA-G deglucosylation. Using cross-species RNA interference, we have shown that Mm_bGlc17 reduces TA-G toxicity. Furthermore, Mm_bGlc17 is required for the preference of M. melolontha larvae for TA-G-deficient plants. Thus, herbivore metabolism modulates both the toxicity and deterrence of a plant defense compound. Our work illustrates the multifaceted roles of insect digestive enzymes as mediators of plant-herbivore interactions.Meret HuberThomas RoderSandra IrmischAlexander RiedelSaskia GablenzJulia FrickePeter RahfeldMichael ReicheltChristian PaetzNicole LiechtiLingfei HuZoe BontYe MengWei HuangChristelle AM RobertJonathan GershenzonMatthias ErbeLife Sciences Publications LtdarticleMelolontha melolonthaTaraxacum officinaleplant defenseroot herbivoresesquiterpene lactoneβ-glucosidaseMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Melolontha melolontha
Taraxacum officinale
plant defense
root herbivore
sesquiterpene lactone
β-glucosidase
Medicine
R
Science
Q
Biology (General)
QH301-705.5
spellingShingle Melolontha melolontha
Taraxacum officinale
plant defense
root herbivore
sesquiterpene lactone
β-glucosidase
Medicine
R
Science
Q
Biology (General)
QH301-705.5
Meret Huber
Thomas Roder
Sandra Irmisch
Alexander Riedel
Saskia Gablenz
Julia Fricke
Peter Rahfeld
Michael Reichelt
Christian Paetz
Nicole Liechti
Lingfei Hu
Zoe Bont
Ye Meng
Wei Huang
Christelle AM Robert
Jonathan Gershenzon
Matthias Erb
A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite
description Gut enzymes can metabolize plant defense compounds and thereby affect the growth and fitness of insect herbivores. Whether these enzymes also influence feeding preference is largely unknown. We studied the metabolization of taraxinic acid β-D-glucopyranosyl ester (TA-G), a sesquiterpene lactone of the common dandelion (Taraxacum officinale) that deters its major root herbivore, the common cockchafer larva (Melolontha melolontha). We have demonstrated that TA-G is rapidly deglucosylated and conjugated to glutathione in the insect gut. A broad-spectrum M. melolontha β-glucosidase, Mm_bGlc17, is sufficient and necessary for TA-G deglucosylation. Using cross-species RNA interference, we have shown that Mm_bGlc17 reduces TA-G toxicity. Furthermore, Mm_bGlc17 is required for the preference of M. melolontha larvae for TA-G-deficient plants. Thus, herbivore metabolism modulates both the toxicity and deterrence of a plant defense compound. Our work illustrates the multifaceted roles of insect digestive enzymes as mediators of plant-herbivore interactions.
format article
author Meret Huber
Thomas Roder
Sandra Irmisch
Alexander Riedel
Saskia Gablenz
Julia Fricke
Peter Rahfeld
Michael Reichelt
Christian Paetz
Nicole Liechti
Lingfei Hu
Zoe Bont
Ye Meng
Wei Huang
Christelle AM Robert
Jonathan Gershenzon
Matthias Erb
author_facet Meret Huber
Thomas Roder
Sandra Irmisch
Alexander Riedel
Saskia Gablenz
Julia Fricke
Peter Rahfeld
Michael Reichelt
Christian Paetz
Nicole Liechti
Lingfei Hu
Zoe Bont
Ye Meng
Wei Huang
Christelle AM Robert
Jonathan Gershenzon
Matthias Erb
author_sort Meret Huber
title A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite
title_short A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite
title_full A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite
title_fullStr A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite
title_full_unstemmed A beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite
title_sort beta-glucosidase of an insect herbivore determines both toxicity and deterrence of a dandelion defense metabolite
publisher eLife Sciences Publications Ltd
publishDate 2021
url https://doaj.org/article/a447ed9d0bc24028bd2ac0f7ba657670
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