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

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

© The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 68(2017), 9 vom: 01. Apr., Seite 2187-2197
1. Verfasser: Li, Xin (VerfasserIn)
Weitere Verfasser: Michlmayr, Herbert, Schweiger, Wolfgang, Malachova, Alexandra, Shin, Sanghyun, Huang, Yadong, Dong, Yanhong, Wiesenberger, Gerlinde, McCormick, Susan, Lemmens, Marc, Fruhmann, Philipp, Hametner, Christian, Berthiller, Franz, Adam, Gerhard, Muehlbauer, Gary J
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, Non-U.S. Gov't Fusarium Head Blight Fusarium graminearum UDP-glycosyltransferase nivalenol trichothecene wheat. Plant Proteins mehr... Trichothecenes 5WOP02RM1U Glucosyltransferases EC 2.4.1.- HvUGT13248 protein, barley
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520 |a © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, U.S. Gov't, Non-P.H.S. 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Fusarium Head Blight 
650 4 |a Fusarium graminearum 
650 4 |a UDP-glycosyltransferase 
650 4 |a nivalenol 
650 4 |a trichothecene 
650 4 |a wheat. 
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650 7 |a Trichothecenes  |2 NLM 
650 7 |a nivalenol  |2 NLM 
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650 7 |a Glucosyltransferases  |2 NLM 
650 7 |a EC 2.4.1.-  |2 NLM 
650 7 |a HvUGT13248 protein, barley  |2 NLM 
650 7 |a EC 2.4.1.-  |2 NLM 
700 1 |a Michlmayr, Herbert  |e verfasserin  |4 aut 
700 1 |a Schweiger, Wolfgang  |e verfasserin  |4 aut 
700 1 |a Malachova, Alexandra  |e verfasserin  |4 aut 
700 1 |a Shin, Sanghyun  |e verfasserin  |4 aut 
700 1 |a Huang, Yadong  |e verfasserin  |4 aut 
700 1 |a Dong, Yanhong  |e verfasserin  |4 aut 
700 1 |a Wiesenberger, Gerlinde  |e verfasserin  |4 aut 
700 1 |a McCormick, Susan  |e verfasserin  |4 aut 
700 1 |a Lemmens, Marc  |e verfasserin  |4 aut 
700 1 |a Fruhmann, Philipp  |e verfasserin  |4 aut 
700 1 |a Hametner, Christian  |e verfasserin  |4 aut 
700 1 |a Berthiller, Franz  |e verfasserin  |4 aut 
700 1 |a Adam, Gerhard  |e verfasserin  |4 aut 
700 1 |a Muehlbauer, Gary J  |e verfasserin  |4 aut 
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