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Dissimilar Crystal Proteins Cry5Ca1 and Cry5Da1 Synergistically Act against Meloidogyne incognita and Delay Cry5Ba-Based Nematode Resistance.

Identifieur interne : 000C74 ( Main/Exploration ); précédent : 000C73; suivant : 000C75

Dissimilar Crystal Proteins Cry5Ca1 and Cry5Da1 Synergistically Act against Meloidogyne incognita and Delay Cry5Ba-Based Nematode Resistance.

Auteurs : Ce Geng [République populaire de Chine] ; Yingying Liu [République populaire de Chine] ; Miaomiao Li [République populaire de Chine] ; Zhen Tang [République populaire de Chine] ; Sajid Muhammad [République populaire de Chine] ; Jinshui Zheng [République populaire de Chine] ; Danfeng Wan [République populaire de Chine] ; Donghai Peng [République populaire de Chine] ; Lifang Ruan [République populaire de Chine] ; Ming Sun [République populaire de Chine]

Source :

RBID : pubmed:28710264

Descripteurs français

English descriptors

Abstract

Cry proteins of Bacillus thuringiensis (Bt) have been successfully used as biopesticides and in transgenic crops throughout the world. However, resources against the most serious agricultural pathogens, plant root-knot nematodes, are limited. The genomes of several highly nematicidal virulent Bt strains from our laboratory have been sequenced, facilitating the identification of novel Cry proteins and other virulence factors. We identified two novel Cry proteins, Cry5Ca1 and Cry5Da1, that exhibit high toxicity against Meloidogyne incognita Using the Caenorhabditis elegans model, the two Cry5 toxins were shown to negatively affect nematode life span, fertility, and survival. The 50% lethal concentrations (LC50s) of Cry5Ca1 and Cry5Da1 were 57.22 μg/ml and 36.69 μg/ml, respectively. Moreover, a synergistic effect (synergism factor, 1.61 to 2.04) was observed for nematicidal toxicity of Cry5Ca1 and Cry5Da1, which is accordant with the phylogenetic results suggesting that domain II of the two novel Cry5 toxins evolved into two independent clades. Through comparison of the depressed degree of toxicity in the β-methylgalactoside detoxification test, we found that the novel toxin Cry5D possesses a different galactose-binding epitope; meanwhile, the finding that Cry5D does not share a motif (GXXXE) in the corresponding loop of domain II with Cry5B could explain the different galactose binding performance. Additionally, low-level cross-resistance of C. elegans bre mutant strains was evident between Cry5B and Cry5D. These results suggest that Cry5D can be used as an alternative to delay the potential resistance of nematodes to Cry5B.IMPORTANCE Although proper gene resources for Bt crops against the most serious agricultural pathogens, plant root-knot nematodes, are limited, we have identified two novel nematicidal toxins, Cry5Ca1 and Cry5Da1, against M. incognita, which have supplied more gene candidates for Bt crops designed against nematodes. Moreover, the association of the dissimilarity between Cry5Da1 and Cry5Ba1 and their low cross-resistance can be attributed not only to a low sequence similarity of domain II but also to the structural difference of the key motif and receptor-binding epitope in the loops. This association facilitates the selection of a proper candidate for the prospective design of pyramided Bt crops that can delay potential resistance.

DOI: 10.1128/AEM.03505-16
PubMed: 28710264
PubMed Central: PMC5583498


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<term>Bacterial Proteins (chemistry)</term>
<term>Bacterial Proteins (pharmacology)</term>
<term>Caenorhabditis elegans (drug effects)</term>
<term>Caenorhabditis elegans (genetics)</term>
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<term>Protéines bactériennes (composition chimique)</term>
<term>Protéines bactériennes (pharmacologie)</term>
<term>Résistance aux substances (MeSH)</term>
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<term>Bacterial Proteins</term>
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<term>Endotoxines</term>
<term>Hémolysines</term>
<term>Protéines bactériennes</term>
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<term>Caenorhabditis elegans</term>
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<term>Caenorhabditis elegans</term>
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<term>Caenorhabditis elegans</term>
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<term>Caenorhabditis elegans</term>
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<term>Hémolysines</term>
<term>Protéines bactériennes</term>
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<term>Animals</term>
<term>Drug Resistance</term>
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<div type="abstract" xml:lang="en">Cry proteins of
<i>Bacillus thuringiensis</i>
(Bt) have been successfully used as biopesticides and in transgenic crops throughout the world. However, resources against the most serious agricultural pathogens, plant root-knot nematodes, are limited. The genomes of several highly nematicidal virulent Bt strains from our laboratory have been sequenced, facilitating the identification of novel Cry proteins and other virulence factors. We identified two novel Cry proteins, Cry5Ca1 and Cry5Da1, that exhibit high toxicity against
<i>Meloidogyne incognita</i>
Using the
<i>Caenorhabditis elegans</i>
model, the two Cry5 toxins were shown to negatively affect nematode life span, fertility, and survival. The 50% lethal concentrations (LC
<sub>50</sub>
s) of Cry5Ca1 and Cry5Da1 were 57.22 μg/ml and 36.69 μg/ml, respectively. Moreover, a synergistic effect (synergism factor, 1.61 to 2.04) was observed for nematicidal toxicity of Cry5Ca1 and Cry5Da1, which is accordant with the phylogenetic results suggesting that domain II of the two novel Cry5 toxins evolved into two independent clades. Through comparison of the depressed degree of toxicity in the β-methylgalactoside detoxification test, we found that the novel toxin Cry5D possesses a different galactose-binding epitope; meanwhile, the finding that Cry5D does not share a motif (GXXXE) in the corresponding loop of domain II with Cry5B could explain the different galactose binding performance. Additionally, low-level cross-resistance of
<i>C. elegans bre</i>
mutant strains was evident between Cry5B and Cry5D. These results suggest that Cry5D can be used as an alternative to delay the potential resistance of nematodes to Cry5B.
<b>IMPORTANCE</b>
Although proper gene resources for Bt crops against the most serious agricultural pathogens, plant root-knot nematodes, are limited, we have identified two novel nematicidal toxins, Cry5Ca1 and Cry5Da1, against
<i>M. incognita</i>
, which have supplied more gene candidates for Bt crops designed against nematodes. Moreover, the association of the dissimilarity between Cry5Da1 and Cry5Ba1 and their low cross-resistance can be attributed not only to a low sequence similarity of domain II but also to the structural difference of the key motif and receptor-binding epitope in the loops. This association facilitates the selection of a proper candidate for the prospective design of pyramided Bt crops that can delay potential resistance.</div>
</front>
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<Issue>18</Issue>
<PubDate>
<Year>2017</Year>
<Month>09</Month>
<Day>15</Day>
</PubDate>
</JournalIssue>
<Title>Applied and environmental microbiology</Title>
<ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation>
</Journal>
<ArticleTitle>Dissimilar Crystal Proteins Cry5Ca1 and Cry5Da1 Synergistically Act against Meloidogyne incognita and Delay Cry5Ba-Based Nematode Resistance.</ArticleTitle>
<ELocationID EIdType="pii" ValidYN="Y">e03505-16</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1128/AEM.03505-16</ELocationID>
<Abstract>
<AbstractText>Cry proteins of
<i>Bacillus thuringiensis</i>
(Bt) have been successfully used as biopesticides and in transgenic crops throughout the world. However, resources against the most serious agricultural pathogens, plant root-knot nematodes, are limited. The genomes of several highly nematicidal virulent Bt strains from our laboratory have been sequenced, facilitating the identification of novel Cry proteins and other virulence factors. We identified two novel Cry proteins, Cry5Ca1 and Cry5Da1, that exhibit high toxicity against
<i>Meloidogyne incognita</i>
Using the
<i>Caenorhabditis elegans</i>
model, the two Cry5 toxins were shown to negatively affect nematode life span, fertility, and survival. The 50% lethal concentrations (LC
<sub>50</sub>
s) of Cry5Ca1 and Cry5Da1 were 57.22 μg/ml and 36.69 μg/ml, respectively. Moreover, a synergistic effect (synergism factor, 1.61 to 2.04) was observed for nematicidal toxicity of Cry5Ca1 and Cry5Da1, which is accordant with the phylogenetic results suggesting that domain II of the two novel Cry5 toxins evolved into two independent clades. Through comparison of the depressed degree of toxicity in the β-methylgalactoside detoxification test, we found that the novel toxin Cry5D possesses a different galactose-binding epitope; meanwhile, the finding that Cry5D does not share a motif (GXXXE) in the corresponding loop of domain II with Cry5B could explain the different galactose binding performance. Additionally, low-level cross-resistance of
<i>C. elegans bre</i>
mutant strains was evident between Cry5B and Cry5D. These results suggest that Cry5D can be used as an alternative to delay the potential resistance of nematodes to Cry5B.
<b>IMPORTANCE</b>
Although proper gene resources for Bt crops against the most serious agricultural pathogens, plant root-knot nematodes, are limited, we have identified two novel nematicidal toxins, Cry5Ca1 and Cry5Da1, against
<i>M. incognita</i>
, which have supplied more gene candidates for Bt crops designed against nematodes. Moreover, the association of the dissimilarity between Cry5Da1 and Cry5Ba1 and their low cross-resistance can be attributed not only to a low sequence similarity of domain II but also to the structural difference of the key motif and receptor-binding epitope in the loops. This association facilitates the selection of a proper candidate for the prospective design of pyramided Bt crops that can delay potential resistance.</AbstractText>
<CopyrightInformation>Copyright © 2017 American Society for Microbiology.</CopyrightInformation>
</Abstract>
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<Author ValidYN="Y">
<LastName>Geng</LastName>
<ForeName>Ce</ForeName>
<Initials>C</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Liu</LastName>
<ForeName>Yingying</ForeName>
<Initials>Y</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Li</LastName>
<ForeName>Miaomiao</ForeName>
<Initials>M</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Tang</LastName>
<ForeName>Zhen</ForeName>
<Initials>Z</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Muhammad</LastName>
<ForeName>Sajid</ForeName>
<Initials>S</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Zheng</LastName>
<ForeName>Jinshui</ForeName>
<Initials>J</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
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<LastName>Wan</LastName>
<ForeName>Danfeng</ForeName>
<Initials>D</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Peng</LastName>
<ForeName>Donghai</ForeName>
<Initials>D</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Ruan</LastName>
<ForeName>Lifang</ForeName>
<Initials>L</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Sun</LastName>
<ForeName>Ming</ForeName>
<Initials>M</Initials>
<AffiliationInfo>
<Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China m98sun@mail.hzau.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic">
<Year>2017</Year>
<Month>08</Month>
<Day>31</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>United States</Country>
<MedlineTA>Appl Environ Microbiol</MedlineTA>
<NlmUniqueID>7605801</NlmUniqueID>
<ISSNLinking>0099-2240</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000969">Antinematodal Agents</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D004731">Endotoxins</NameOfSubstance>
</Chemical>
<Chemical>
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<NameOfSubstance UI="D006460">Hemolysin Proteins</NameOfSubstance>
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<Chemical>
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<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D000969" MajorTopicYN="N">Antinematodal Agents</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName>
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<MeshHeading>
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</MeshHeading>
<MeshHeading>
<DescriptorName UI="D017173" MajorTopicYN="N">Caenorhabditis elegans</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D004351" MajorTopicYN="Y">Drug Resistance</DescriptorName>
</MeshHeading>
<MeshHeading>
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</MeshHeading>
<MeshHeading>
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</MeshHeading>
<MeshHeading>
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<Keyword MajorTopicYN="Y">Caenorhabditis elegans</Keyword>
<Keyword MajorTopicYN="Y">Cry proteins</Keyword>
<Keyword MajorTopicYN="Y">bre resistance</Keyword>
<Keyword MajorTopicYN="Y">nematicidal</Keyword>
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