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A quinone-dependent dehydrogenase and two NADPH-dependent aldo/keto reductases detoxify deoxynivalenol in wheat via epimerization in a Devosia strain.

Identifieur interne : 000283 ( Main/Exploration ); précédent : 000282; suivant : 000284

A quinone-dependent dehydrogenase and two NADPH-dependent aldo/keto reductases detoxify deoxynivalenol in wheat via epimerization in a Devosia strain.

Auteurs : Wei-Jie He [République populaire de Chine] ; Meng-Meng Shi [République populaire de Chine] ; Peng Yang [République populaire de Chine] ; Tao Huang [République populaire de Chine] ; Yue Zhao [République populaire de Chine] ; Ai-Bo Wu [République populaire de Chine] ; Wu-Bei Dong [République populaire de Chine] ; He-Ping Li [République populaire de Chine] ; Jing-Bo Zhang [République populaire de Chine] ; Yu-Cai Liao [République populaire de Chine]

Source :

RBID : pubmed:32247890

Descripteurs français

English descriptors

Abstract

The Fusarium mycotoxin deoxynivalenol (DON) is typically controlled by fungicides. Here, we report DON detoxification using enzymes from the highly active Devosia strain D6-9 which degraded DON at 2.5 μg/min/108 cells. Strain D6-9 catabolized DON to 3-keto-DON and 3-epi-DON, completely removing DON in wheat. Genome analysis of three Devosia strains (D6-9, D17, and D13584), with strain D6-9 transcriptomes, identified three genes responsible for DON epimerization. One gene encodes a quinone-dependent DON dehydrogenase QDDH which oxidized DON into 3-keto-DON. Two genes encode the NADPH-dependent aldo/keto reductases AKR13B2 and AKR6D1 that convert 3-keto-DON into 3-epi-DON. Recombinant proteins expressed in Escherichia coli efficiently degraded DON in wheat grains. Molecular docking and site-directed mutagenesis revealed that residues S497, E499, and E535 function in QDDH's DON-oxidizing activity. These results advance potential microbial and enzymatic elimination of DON in agricultural samples and lend insight into the underlying mechanisms and molecular evolution of DON detoxification.

DOI: 10.1016/j.foodchem.2020.126703
PubMed: 32247890


Affiliations:


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<term>Aldo-Keto Reductases (metabolism)</term>
<term>Fusarium (metabolism)</term>
<term>Hyphomicrobiaceae (enzymology)</term>
<term>Molecular Docking Simulation (MeSH)</term>
<term>NADP (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Quinone Reductases (metabolism)</term>
<term>Trichothecenes (metabolism)</term>
<term>Triticum (enzymology)</term>
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<term>Aldo-keto reductases (métabolisme)</term>
<term>Fusarium (métabolisme)</term>
<term>Hyphomicrobiaceae (enzymologie)</term>
<term>NADP (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Quinone reductases (métabolisme)</term>
<term>Simulation de docking moléculaire (MeSH)</term>
<term>Trichothécènes (métabolisme)</term>
<term>Triticum (enzymologie)</term>
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<term>Aldo-Keto Reductases</term>
<term>NADP</term>
<term>Quinone Reductases</term>
<term>Trichothecenes</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr">
<term>Hyphomicrobiaceae</term>
<term>Triticum</term>
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<term>Hyphomicrobiaceae</term>
<term>Triticum</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Fusarium</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Aldo-keto reductases</term>
<term>Fusarium</term>
<term>NADP</term>
<term>Quinone reductases</term>
<term>Trichothécènes</term>
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<term>Molecular Docking Simulation</term>
<term>Oxidation-Reduction</term>
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<term>Oxydoréduction</term>
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<div type="abstract" xml:lang="en">The Fusarium mycotoxin deoxynivalenol (DON) is typically controlled by fungicides. Here, we report DON detoxification using enzymes from the highly active Devosia strain D6-9 which degraded DON at 2.5 μg/min/10
<sup>8</sup>
cells. Strain D6-9 catabolized DON to 3-keto-DON and 3-epi-DON, completely removing DON in wheat. Genome analysis of three Devosia strains (D6-9, D17, and D13584), with strain D6-9 transcriptomes, identified three genes responsible for DON epimerization. One gene encodes a quinone-dependent DON dehydrogenase QDDH which oxidized DON into 3-keto-DON. Two genes encode the NADPH-dependent aldo/keto reductases AKR13B2 and AKR6D1 that convert 3-keto-DON into 3-epi-DON. Recombinant proteins expressed in Escherichia coli efficiently degraded DON in wheat grains. Molecular docking and site-directed mutagenesis revealed that residues S497, E499, and E535 function in QDDH's DON-oxidizing activity. These results advance potential microbial and enzymatic elimination of DON in agricultural samples and lend insight into the underlying mechanisms and molecular evolution of DON detoxification.</div>
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<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.foodchem.2020.126703</ELocationID>
<Abstract>
<AbstractText>The Fusarium mycotoxin deoxynivalenol (DON) is typically controlled by fungicides. Here, we report DON detoxification using enzymes from the highly active Devosia strain D6-9 which degraded DON at 2.5 μg/min/10
<sup>8</sup>
cells. Strain D6-9 catabolized DON to 3-keto-DON and 3-epi-DON, completely removing DON in wheat. Genome analysis of three Devosia strains (D6-9, D17, and D13584), with strain D6-9 transcriptomes, identified three genes responsible for DON epimerization. One gene encodes a quinone-dependent DON dehydrogenase QDDH which oxidized DON into 3-keto-DON. Two genes encode the NADPH-dependent aldo/keto reductases AKR13B2 and AKR6D1 that convert 3-keto-DON into 3-epi-DON. Recombinant proteins expressed in Escherichia coli efficiently degraded DON in wheat grains. Molecular docking and site-directed mutagenesis revealed that residues S497, E499, and E535 function in QDDH's DON-oxidizing activity. These results advance potential microbial and enzymatic elimination of DON in agricultural samples and lend insight into the underlying mechanisms and molecular evolution of DON detoxification.</AbstractText>
<CopyrightInformation>Copyright © 2020 Elsevier Ltd. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>He</LastName>
<ForeName>Wei-Jie</ForeName>
<Initials>WJ</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; Hubei Engineering and Technology Research Center of Wheat/Wheat Disease Biology Research Station for Central China, Food Crops Institute, Hubei Academy of Agricultural Sciences, Wuhan 430064, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Shi</LastName>
<ForeName>Meng-Meng</ForeName>
<Initials>MM</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Yang</LastName>
<ForeName>Peng</ForeName>
<Initials>P</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Huang</LastName>
<ForeName>Tao</ForeName>
<Initials>T</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Zhao</LastName>
<ForeName>Yue</ForeName>
<Initials>Y</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Wu</LastName>
<ForeName>Ai-Bo</ForeName>
<Initials>AB</Initials>
<AffiliationInfo>
<Affiliation>Key Laboratory of Food Safety Research Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Dong</LastName>
<ForeName>Wu-Bei</ForeName>
<Initials>WB</Initials>
<AffiliationInfo>
<Affiliation>College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Li</LastName>
<ForeName>He-Ping</ForeName>
<Initials>HP</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Zhang</LastName>
<ForeName>Jing-Bo</ForeName>
<Initials>JB</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China. Electronic address: jingbozhang@mail.hzau.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Liao</LastName>
<ForeName>Yu-Cai</ForeName>
<Initials>YC</Initials>
<AffiliationInfo>
<Affiliation>Molecular Biotechnology Laboratory of Triticeae Crops, Huazhong Agricultural University, Wuhan 430070, People's Republic of China; College of Plant Science and Technology, Huazhong Agricultural University, Wuhan 430070, People's Republic of China. Electronic address: yucailiao@mail.hzau.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic">
<Year>2020</Year>
<Month>03</Month>
<Day>27</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>England</Country>
<MedlineTA>Food Chem</MedlineTA>
<NlmUniqueID>7702639</NlmUniqueID>
<ISSNLinking>0308-8146</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C000609395">3-keto-deoxynivalenol</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014255">Trichothecenes</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>53-59-8</RegistryNumber>
<NameOfSubstance UI="D009249">NADP</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>EC 1.1.1.-</RegistryNumber>
<NameOfSubstance UI="D000074408">Aldo-Keto Reductases</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>EC 1.6.99.-</RegistryNumber>
<NameOfSubstance UI="D011808">Quinone Reductases</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>JT37HYP23V</RegistryNumber>
<NameOfSubstance UI="C007262">deoxynivalenol</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D000074408" MajorTopicYN="N">Aldo-Keto Reductases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D005670" MajorTopicYN="N">Fusarium</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D041921" MajorTopicYN="N">Hyphomicrobiaceae</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D062105" MajorTopicYN="N">Molecular Docking Simulation</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D011808" MajorTopicYN="N">Quinone Reductases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D014255" MajorTopicYN="N">Trichothecenes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D014908" MajorTopicYN="N">Triticum</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM">
<Keyword MajorTopicYN="N">3-epi-deoxynivalenol (PubChem CID 13456592)</Keyword>
<Keyword MajorTopicYN="N">Alcohol dehydrogenase</Keyword>
<Keyword MajorTopicYN="N">Aldo/keto reductases</Keyword>
<Keyword MajorTopicYN="N">Deoxynivalenol (PubChem CID 40024)</Keyword>
<Keyword MajorTopicYN="N">Deoxynivalenol epimerization</Keyword>
<Keyword MajorTopicYN="N">Enzymatic detoxification</Keyword>
<Keyword MajorTopicYN="N">Molecular docking</Keyword>
<Keyword MajorTopicYN="N">NADPH (PubChem CID 5884)</Keyword>
<Keyword MajorTopicYN="N">Pyrroloquinoline quinone (PubChem CID 1024)</Keyword>
</KeywordList>
<CoiStatement>Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.</CoiStatement>
</MedlineCitation>
<PubmedData>
<History>
<PubMedPubDate PubStatus="received">
<Year>2019</Year>
<Month>01</Month>
<Day>20</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised">
<Year>2020</Year>
<Month>03</Month>
<Day>26</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2020</Year>
<Month>03</Month>
<Day>26</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed">
<Year>2020</Year>
<Month>4</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="medline">
<Year>2020</Year>
<Month>7</Month>
<Day>8</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="entrez">
<Year>2020</Year>
<Month>4</Month>
<Day>6</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
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<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">32247890</ArticleId>
<ArticleId IdType="pii">S0308-8146(20)30565-3</ArticleId>
<ArticleId IdType="doi">10.1016/j.foodchem.2020.126703</ArticleId>
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</pubmed>
<affiliations>
<list>
<country>
<li>République populaire de Chine</li>
</country>
<region>
<li>Hubei</li>
</region>
<settlement>
<li>Wuhan</li>
</settlement>
</list>
<tree>
<country name="République populaire de Chine">
<region name="Hubei">
<name sortKey="He, Wei Jie" sort="He, Wei Jie" uniqKey="He W" first="Wei-Jie" last="He">Wei-Jie He</name>
</region>
<name sortKey="Dong, Wu Bei" sort="Dong, Wu Bei" uniqKey="Dong W" first="Wu-Bei" last="Dong">Wu-Bei Dong</name>
<name sortKey="Huang, Tao" sort="Huang, Tao" uniqKey="Huang T" first="Tao" last="Huang">Tao Huang</name>
<name sortKey="Li, He Ping" sort="Li, He Ping" uniqKey="Li H" first="He-Ping" last="Li">He-Ping Li</name>
<name sortKey="Liao, Yu Cai" sort="Liao, Yu Cai" uniqKey="Liao Y" first="Yu-Cai" last="Liao">Yu-Cai Liao</name>
<name sortKey="Shi, Meng Meng" sort="Shi, Meng Meng" uniqKey="Shi M" first="Meng-Meng" last="Shi">Meng-Meng Shi</name>
<name sortKey="Wu, Ai Bo" sort="Wu, Ai Bo" uniqKey="Wu A" first="Ai-Bo" last="Wu">Ai-Bo Wu</name>
<name sortKey="Yang, Peng" sort="Yang, Peng" uniqKey="Yang P" first="Peng" last="Yang">Peng Yang</name>
<name sortKey="Zhang, Jing Bo" sort="Zhang, Jing Bo" uniqKey="Zhang J" first="Jing-Bo" last="Zhang">Jing-Bo Zhang</name>
<name sortKey="Zhao, Yue" sort="Zhao, Yue" uniqKey="Zhao Y" first="Yue" last="Zhao">Yue Zhao</name>
</country>
</tree>
</affiliations>
</record>

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