A barley UDP-glucosyltransferase inactivates nivalenol and provides Fusarium Head Blight resistance in transgenic wheat

Xin Li; Herbert Michlmayr; Wolfgang Schweiger; Alexandra Malachova; Sanghyun Shin; Yadong Huang; Yanhong Dong; Gerlinde Wiesenberger; Susan McCormick; Marc Lemmens; Philipp Fruhmann; Christian Hametner; Franz Berthiller; Gerhard Adam; Gary J. Muehlbauer

doi:10.1093/jxb/erx109

A barley UDP-glucosyltransferase inactivates nivalenol and provides Fusarium Head Blight resistance in transgenic wheat

Xin Li, Herbert Michlmayr, Wolfgang Schweiger, Alexandra Malachova, Sanghyun Shin, Yadong Huang, Yanhong Dong, Gerlinde Wiesenberger, Susan McCormick, Marc Lemmens, Philipp Fruhmann, Christian Hametner, Franz Berthiller, Gerhard Adam, Gary J. Muehlbauer

Research output: Contribution to journal › Article › peer-review

63 Scopus citations

Abstract

Fusarium Head Blight is a disease of cereal crops that causes severe yield losses and mycotoxin contamination of grain. The main causal pathogen, Fusarium graminearum, produces the trichothecene toxins deoxynivalenol or nivalenol as virulence factors. Nivalenol-producing isolates are most prevalent in Asia but co-exist with deoxynivalenol producers in lower frequency in North America and Europe. Previous studies identified a barley UDP-glucosyltransferase, HvUGT13248, that efficiently detoxifies deoxynivalenol, and when expressed in transgenic wheat results in high levels of type II resistance against deoxynivalenol-producing F. graminearum. Here we show that HvUGT13248 is also capable of converting nivalenol into the non-Toxic nivalenol-3-O-β-d-glucoside. We describe the enzymatic preparation of a nivalenol-glucoside standard and its use in development of an analytical method to detect the nivalenol-glucoside conjugate. Recombinant Escherichia coli expressing HvUGT13248 glycosylates nivalenol more efficiently than deoxynivalenol. Overexpression in yeast, Arabidopsis thaliana, and wheat leads to increased nivalenol resistance. Increased ability to convert nivalenol to nivalenol-glucoside was observed in transgenic wheat, which also exhibits type II resistance to a nivalenol-producing F. graminearum strain. Our results demonstrate the HvUGT13248 can act to detoxify deoxynivalenol and nivalenol and provide resistance to deoxynivalenol-And nivalenol-producing Fusarium.

Original language	English (US)
Pages (from-to)	2187-2197
Number of pages	11
Journal	Journal of experimental botany
Volume	68
Issue number	9
DOIs	https://doi.org/10.1093/jxb/erx109
State	Published - Apr 1 2017

Bibliographical note

Funding Information:
This material is based upon work supported by the US Department of Agriculture, under Agreement no. 59-0206-4-021. This is a co-operative project with the US Wheat and Barley Scab Initiative. Any opinions, findings, conclusions, or recommendations expressed in this publication are those of the authors and do not necessarily reflect the view of the US Department of Agriculture. The work performed in Austria was funded by the FWF special research project Fusarium (F3708, F3706, F3711, and F3715) and the Vienna Science and Technology Fund (LS12-021). Furthermore, we thank the Austrian Federal Ministry of Science, Research and Economy, the Austrian National Foundation of Research, Technology and Development, as well as the BIOMIN Holding GmbH for funding the Christian Doppler Laboratory for Mycotoxin Metabolism. We also thank H. Corby Kistler for the NIV-producing Fusarium graminearum strain

Publisher Copyright:
© The Author 2017.

Keywords

Fusarium graminearum
Fusarium head blight
Nivalenol
Trichothecene
UDP-glycosyltransferase
Wheat

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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Li, X., Michlmayr, H., Schweiger, W., Malachova, A., Shin, S., Huang, Y., Dong, Y., Wiesenberger, G., McCormick, S., Lemmens, M., Fruhmann, P., Hametner, C., Berthiller, F., Adam, G., & Muehlbauer, G. J. (2017). A barley UDP-glucosyltransferase inactivates nivalenol and provides Fusarium Head Blight resistance in transgenic wheat. Journal of experimental botany, 68(9), 2187-2197. https://doi.org/10.1093/jxb/erx109

Li, X, Michlmayr, H, Schweiger, W, Malachova, A, Shin, S, Huang, Y, Dong, Y, Wiesenberger, G, McCormick, S, Lemmens, M, Fruhmann, P, Hametner, C, Berthiller, F, Adam, G & Muehlbauer, GJ 2017, 'A barley UDP-glucosyltransferase inactivates nivalenol and provides Fusarium Head Blight resistance in transgenic wheat', Journal of experimental botany, vol. 68, no. 9, pp. 2187-2197. https://doi.org/10.1093/jxb/erx109

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abstract = "Fusarium Head Blight is a disease of cereal crops that causes severe yield losses and mycotoxin contamination of grain. The main causal pathogen, Fusarium graminearum, produces the trichothecene toxins deoxynivalenol or nivalenol as virulence factors. Nivalenol-producing isolates are most prevalent in Asia but co-exist with deoxynivalenol producers in lower frequency in North America and Europe. Previous studies identified a barley UDP-glucosyltransferase, HvUGT13248, that efficiently detoxifies deoxynivalenol, and when expressed in transgenic wheat results in high levels of type II resistance against deoxynivalenol-producing F. graminearum. Here we show that HvUGT13248 is also capable of converting nivalenol into the non-Toxic nivalenol-3-O-β-d-glucoside. We describe the enzymatic preparation of a nivalenol-glucoside standard and its use in development of an analytical method to detect the nivalenol-glucoside conjugate. Recombinant Escherichia coli expressing HvUGT13248 glycosylates nivalenol more efficiently than deoxynivalenol. Overexpression in yeast, Arabidopsis thaliana, and wheat leads to increased nivalenol resistance. Increased ability to convert nivalenol to nivalenol-glucoside was observed in transgenic wheat, which also exhibits type II resistance to a nivalenol-producing F. graminearum strain. Our results demonstrate the HvUGT13248 can act to detoxify deoxynivalenol and nivalenol and provide resistance to deoxynivalenol-And nivalenol-producing Fusarium.",

keywords = "Fusarium graminearum, Fusarium head blight, Nivalenol, Trichothecene, UDP-glycosyltransferase, Wheat",

author = "Xin Li and Herbert Michlmayr and Wolfgang Schweiger and Alexandra Malachova and Sanghyun Shin and Yadong Huang and Yanhong Dong and Gerlinde Wiesenberger and Susan McCormick and Marc Lemmens and Philipp Fruhmann and Christian Hametner and Franz Berthiller and Gerhard Adam and Muehlbauer, {Gary J.}",

note = "Funding Information: This material is based upon work supported by the US Department of Agriculture, under Agreement no. 59-0206-4-021. This is a co-operative project with the US Wheat and Barley Scab Initiative. Any opinions, findings, conclusions, or recommendations expressed in this publication are those of the authors and do not necessarily reflect the view of the US Department of Agriculture. The work performed in Austria was funded by the FWF special research project Fusarium (F3708, F3706, F3711, and F3715) and the Vienna Science and Technology Fund (LS12-021). Furthermore, we thank the Austrian Federal Ministry of Science, Research and Economy, the Austrian National Foundation of Research, Technology and Development, as well as the BIOMIN Holding GmbH for funding the Christian Doppler Laboratory for Mycotoxin Metabolism. We also thank H. Corby Kistler for the NIV-producing Fusarium graminearum strain Publisher Copyright: {\textcopyright} The Author 2017.",

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T1 - A barley UDP-glucosyltransferase inactivates nivalenol and provides Fusarium Head Blight resistance in transgenic wheat

AU - Li, Xin

AU - Michlmayr, Herbert

AU - Schweiger, Wolfgang

AU - Malachova, Alexandra

AU - Shin, Sanghyun

AU - Huang, Yadong

AU - Dong, Yanhong

AU - Wiesenberger, Gerlinde

AU - McCormick, Susan

AU - Lemmens, Marc

AU - Fruhmann, Philipp

AU - Hametner, Christian

AU - Berthiller, Franz

AU - Adam, Gerhard

AU - Muehlbauer, Gary J.

N1 - Funding Information: This material is based upon work supported by the US Department of Agriculture, under Agreement no. 59-0206-4-021. This is a co-operative project with the US Wheat and Barley Scab Initiative. Any opinions, findings, conclusions, or recommendations expressed in this publication are those of the authors and do not necessarily reflect the view of the US Department of Agriculture. The work performed in Austria was funded by the FWF special research project Fusarium (F3708, F3706, F3711, and F3715) and the Vienna Science and Technology Fund (LS12-021). Furthermore, we thank the Austrian Federal Ministry of Science, Research and Economy, the Austrian National Foundation of Research, Technology and Development, as well as the BIOMIN Holding GmbH for funding the Christian Doppler Laboratory for Mycotoxin Metabolism. We also thank H. Corby Kistler for the NIV-producing Fusarium graminearum strain Publisher Copyright: © The Author 2017.

PY - 2017/4/1

Y1 - 2017/4/1

N2 - Fusarium Head Blight is a disease of cereal crops that causes severe yield losses and mycotoxin contamination of grain. The main causal pathogen, Fusarium graminearum, produces the trichothecene toxins deoxynivalenol or nivalenol as virulence factors. Nivalenol-producing isolates are most prevalent in Asia but co-exist with deoxynivalenol producers in lower frequency in North America and Europe. Previous studies identified a barley UDP-glucosyltransferase, HvUGT13248, that efficiently detoxifies deoxynivalenol, and when expressed in transgenic wheat results in high levels of type II resistance against deoxynivalenol-producing F. graminearum. Here we show that HvUGT13248 is also capable of converting nivalenol into the non-Toxic nivalenol-3-O-β-d-glucoside. We describe the enzymatic preparation of a nivalenol-glucoside standard and its use in development of an analytical method to detect the nivalenol-glucoside conjugate. Recombinant Escherichia coli expressing HvUGT13248 glycosylates nivalenol more efficiently than deoxynivalenol. Overexpression in yeast, Arabidopsis thaliana, and wheat leads to increased nivalenol resistance. Increased ability to convert nivalenol to nivalenol-glucoside was observed in transgenic wheat, which also exhibits type II resistance to a nivalenol-producing F. graminearum strain. Our results demonstrate the HvUGT13248 can act to detoxify deoxynivalenol and nivalenol and provide resistance to deoxynivalenol-And nivalenol-producing Fusarium.

AB - Fusarium Head Blight is a disease of cereal crops that causes severe yield losses and mycotoxin contamination of grain. The main causal pathogen, Fusarium graminearum, produces the trichothecene toxins deoxynivalenol or nivalenol as virulence factors. Nivalenol-producing isolates are most prevalent in Asia but co-exist with deoxynivalenol producers in lower frequency in North America and Europe. Previous studies identified a barley UDP-glucosyltransferase, HvUGT13248, that efficiently detoxifies deoxynivalenol, and when expressed in transgenic wheat results in high levels of type II resistance against deoxynivalenol-producing F. graminearum. Here we show that HvUGT13248 is also capable of converting nivalenol into the non-Toxic nivalenol-3-O-β-d-glucoside. We describe the enzymatic preparation of a nivalenol-glucoside standard and its use in development of an analytical method to detect the nivalenol-glucoside conjugate. Recombinant Escherichia coli expressing HvUGT13248 glycosylates nivalenol more efficiently than deoxynivalenol. Overexpression in yeast, Arabidopsis thaliana, and wheat leads to increased nivalenol resistance. Increased ability to convert nivalenol to nivalenol-glucoside was observed in transgenic wheat, which also exhibits type II resistance to a nivalenol-producing F. graminearum strain. Our results demonstrate the HvUGT13248 can act to detoxify deoxynivalenol and nivalenol and provide resistance to deoxynivalenol-And nivalenol-producing Fusarium.

KW - Fusarium graminearum

KW - Fusarium head blight

KW - Nivalenol

KW - Trichothecene

KW - UDP-glycosyltransferase

KW - Wheat

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ER -

A barley UDP-glucosyltransferase inactivates nivalenol and provides Fusarium Head Blight resistance in transgenic wheat

Abstract

Bibliographical note

Keywords

UN SDGs

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