Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol Detoxification
Oat is susceptible to several Fusarium species that cause contamination with different trichothecene mycotoxins. The molecular mechanisms behind Fusarium resistance in oat have yet to be elucidated. In the present work, we identified and characterised two oat UDP-glucosyltransferases orthologous to...
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MDPI AG
2022-06-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/14/7/446 |
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| author | Alfia Khairullina Nikos Tsardakas Renhuldt Gerlinde Wiesenberger Johan Bentzer David B. Collinge Gerhard Adam Leif Bülow |
| author_facet | Alfia Khairullina Nikos Tsardakas Renhuldt Gerlinde Wiesenberger Johan Bentzer David B. Collinge Gerhard Adam Leif Bülow |
| author_sort | Alfia Khairullina |
| collection | DOAJ |
| description | Oat is susceptible to several Fusarium species that cause contamination with different trichothecene mycotoxins. The molecular mechanisms behind Fusarium resistance in oat have yet to be elucidated. In the present work, we identified and characterised two oat UDP-glucosyltransferases orthologous to barley HvUGT13248. Overexpression of the latter in wheat had been shown previously to increase resistance to deoxynivalenol (DON) and nivalenol (NIV) and to decrease disease the severity of both Fusarium head blight and Fusarium crown rot. Both oat genes are highly inducible by the application of DON and during infection with <i>Fusarium graminearum</i>. Heterologous expression of these genes in a toxin-sensitive strain of <i>Saccharomyces cerevisiae</i> conferred high levels of resistance to DON, NIV and HT-2 toxins, but not C4-acetylated trichothecenes (T-2, diacetoxyscirpenol). Recombinant enzymes AsUGT1 and AsUGT2 expressed in <i>Escherichia coli</i> rapidly lost activity upon purification, but the treatment of whole cells with the toxin clearly demonstrated the ability to convert DON into DON-3-O-glucoside. The two UGTs could therefore play an important role in counteracting the Fusarium virulence factor DON in oat. |
| first_indexed | 2024-03-09T10:11:19Z |
| format | Article |
| id | doaj.art-30308fae227748978e930147d4ab4f80 |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-03-09T10:11:19Z |
| publishDate | 2022-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-30308fae227748978e930147d4ab4f802023-12-01T22:45:28ZengMDPI AGToxins2072-66512022-06-0114744610.3390/toxins14070446Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol DetoxificationAlfia Khairullina0Nikos Tsardakas Renhuldt1Gerlinde Wiesenberger2Johan Bentzer3David B. Collinge4Gerhard Adam5Leif Bülow6Division of Pure and Applied Biochemistry, Lund University, 221 00 Lund, SwedenDivision of Pure and Applied Biochemistry, Lund University, 221 00 Lund, SwedenInstitute of Microbial Genetics, Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Konrad Lorenz Str. 24, 3430 Tulln, AustriaDivision of Pure and Applied Biochemistry, Lund University, 221 00 Lund, SwedenDepartment of Plant and Environmental Sciences, University of Copenhagen, 1871 Frederiksberg, DenmarkInstitute of Microbial Genetics, Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Konrad Lorenz Str. 24, 3430 Tulln, AustriaDivision of Pure and Applied Biochemistry, Lund University, 221 00 Lund, SwedenOat is susceptible to several Fusarium species that cause contamination with different trichothecene mycotoxins. The molecular mechanisms behind Fusarium resistance in oat have yet to be elucidated. In the present work, we identified and characterised two oat UDP-glucosyltransferases orthologous to barley HvUGT13248. Overexpression of the latter in wheat had been shown previously to increase resistance to deoxynivalenol (DON) and nivalenol (NIV) and to decrease disease the severity of both Fusarium head blight and Fusarium crown rot. Both oat genes are highly inducible by the application of DON and during infection with <i>Fusarium graminearum</i>. Heterologous expression of these genes in a toxin-sensitive strain of <i>Saccharomyces cerevisiae</i> conferred high levels of resistance to DON, NIV and HT-2 toxins, but not C4-acetylated trichothecenes (T-2, diacetoxyscirpenol). Recombinant enzymes AsUGT1 and AsUGT2 expressed in <i>Escherichia coli</i> rapidly lost activity upon purification, but the treatment of whole cells with the toxin clearly demonstrated the ability to convert DON into DON-3-O-glucoside. The two UGTs could therefore play an important role in counteracting the Fusarium virulence factor DON in oat.https://www.mdpi.com/2072-6651/14/7/446oatsdeoxynivalenolUDP-glucosyltransferaseglycosylation |
| spellingShingle | Alfia Khairullina Nikos Tsardakas Renhuldt Gerlinde Wiesenberger Johan Bentzer David B. Collinge Gerhard Adam Leif Bülow Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol Detoxification Toxins oats deoxynivalenol UDP-glucosyltransferase glycosylation |
| title | Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol Detoxification |
| title_full | Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol Detoxification |
| title_fullStr | Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol Detoxification |
| title_full_unstemmed | Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol Detoxification |
| title_short | Identification and Functional Characterisation of Two Oat UDP-Glucosyltransferases Involved in Deoxynivalenol Detoxification |
| title_sort | identification and functional characterisation of two oat udp glucosyltransferases involved in deoxynivalenol detoxification |
| topic | oats deoxynivalenol UDP-glucosyltransferase glycosylation |
| url | https://www.mdpi.com/2072-6651/14/7/446 |
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