Binary toxins from Bacillus thuringiensis active against the western corn rootworm, Diabrotica virgifera virgifera LeConte
The western corn rootworm, Diabrotica virgifera virgifera LeConte, is a significant pest of corn in the United States. The development of transgenic corn hybrids resistant to rootworm feeding damage depends on the identification of genes encoding insecticidal proteins toxic to rootworm larvae. In th...
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description | The western corn rootworm, Diabrotica virgifera virgifera LeConte, is a significant pest of corn in the United States. The development of transgenic corn hybrids resistant to rootworm feeding damage depends on the identification of genes encoding insecticidal proteins toxic to rootworm larvae. In this study, a bioassay screen was used to identify several isolates of the bacterium Bacillus thuringiensis active against rootworm. These bacterial isolates each produce distinct crystal proteins with approximate molecular masses of 13 to 15 kDa and 44 kDa. Insect bioassays demonstrated that both protein classes are required for insecticidal activity against this rootworm species. The genes encoding these proteins are organized in apparent operons and are associated with other genes encoding crystal proteins of unknown function. The antirootworm proteins produced by B. thuringiensis strains EG5899 and EG9444 closely resemble previously described crystal proteins of the Cry34A and Cry35A classes. The antirootworm proteins produced by strain EG4851, designated Cry34Ba1 and Cry35Ba1, represent a new binary toxin. Genes encoding these proteins could become an important component of a sustainable resistance management strategy against this insect pest. |
doi_str_mv | 10.1128/AEM.70.8.4889-4898.2004 |
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The development of transgenic corn hybrids resistant to rootworm feeding damage depends on the identification of genes encoding insecticidal proteins toxic to rootworm larvae. In this study, a bioassay screen was used to identify several isolates of the bacterium Bacillus thuringiensis active against rootworm. These bacterial isolates each produce distinct crystal proteins with approximate molecular masses of 13 to 15 kDa and 44 kDa. Insect bioassays demonstrated that both protein classes are required for insecticidal activity against this rootworm species. The genes encoding these proteins are organized in apparent operons and are associated with other genes encoding crystal proteins of unknown function. The antirootworm proteins produced by B. thuringiensis strains EG5899 and EG9444 closely resemble previously described crystal proteins of the Cry34A and Cry35A classes. The antirootworm proteins produced by strain EG4851, designated Cry34Ba1 and Cry35Ba1, represent a new binary toxin. Genes encoding these proteins could become an important component of a sustainable resistance management strategy against this insect pest.</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/AEM.70.8.4889-4898.2004</identifier><identifier>PMID: 15294828</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Animals ; Bacillus thuringiensis ; Bacillus thuringiensis - genetics ; Bacillus thuringiensis - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacterial Proteins - toxicity ; bacterial toxins ; Bacterial Toxins - chemistry ; Bacterial Toxins - genetics ; Bacterial Toxins - metabolism ; Bacterial Toxins - toxicity ; Base Sequence ; bioassays ; Biological and medical sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biopesticides ; Biotechnology ; Cloning, Molecular ; Coleoptera - growth & development ; Corn ; crystal proteins ; Diabrotica virgifera virgifera ; Endotoxins - chemistry ; Endotoxins - genetics ; Endotoxins - metabolism ; Endotoxins - toxicity ; Fundamental and applied biological sciences. Psychology ; genes ; Hemolysin Proteins ; Hybridization ; insect pests ; insecticidal properties ; Larva - growth & development ; larvae ; Microbiology ; Miscellaneous ; Mission oriented research ; Molecular Sequence Data ; molecular weight ; nucleotide sequences ; Pest Control, Biological ; Physiology and Biotechnology ; Proteins ; Sequence Analysis, DNA ; Toxins ; Zea mays - parasitology</subject><ispartof>Applied and Environmental Microbiology, 2004-08, Vol.70 (8), p.4889-4898</ispartof><rights>2005 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Aug 2004</rights><rights>Copyright © 2004, American Society for Microbiology 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c587t-3405f7fb1401c58b3dc97f00cca528a1035988644b2a7e09dfb25438f08da6db3</citedby><cites>FETCH-LOGICAL-c587t-3405f7fb1401c58b3dc97f00cca528a1035988644b2a7e09dfb25438f08da6db3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC492402/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC492402/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,3175,3176,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16006528$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15294828$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Baum, J.A</creatorcontrib><creatorcontrib>Chu, C.R</creatorcontrib><creatorcontrib>Rupar, M</creatorcontrib><creatorcontrib>Brown, G.R</creatorcontrib><creatorcontrib>Donovan, W.P</creatorcontrib><creatorcontrib>Huesing, J.E</creatorcontrib><creatorcontrib>Ilagan, O</creatorcontrib><creatorcontrib>Malvar, T.M</creatorcontrib><creatorcontrib>Pleau, M</creatorcontrib><creatorcontrib>Walters, M</creatorcontrib><title>Binary toxins from Bacillus thuringiensis active against the western corn rootworm, Diabrotica virgifera virgifera LeConte</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>The western corn rootworm, Diabrotica virgifera virgifera LeConte, is a significant pest of corn in the United States. The development of transgenic corn hybrids resistant to rootworm feeding damage depends on the identification of genes encoding insecticidal proteins toxic to rootworm larvae. In this study, a bioassay screen was used to identify several isolates of the bacterium Bacillus thuringiensis active against rootworm. These bacterial isolates each produce distinct crystal proteins with approximate molecular masses of 13 to 15 kDa and 44 kDa. Insect bioassays demonstrated that both protein classes are required for insecticidal activity against this rootworm species. The genes encoding these proteins are organized in apparent operons and are associated with other genes encoding crystal proteins of unknown function. The antirootworm proteins produced by B. thuringiensis strains EG5899 and EG9444 closely resemble previously described crystal proteins of the Cry34A and Cry35A classes. The antirootworm proteins produced by strain EG4851, designated Cry34Ba1 and Cry35Ba1, represent a new binary toxin. Genes encoding these proteins could become an important component of a sustainable resistance management strategy against this insect pest.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Animals</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - genetics</subject><subject>Bacillus thuringiensis - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacterial Proteins - toxicity</subject><subject>bacterial toxins</subject><subject>Bacterial Toxins - chemistry</subject><subject>Bacterial Toxins - genetics</subject><subject>Bacterial Toxins - metabolism</subject><subject>Bacterial Toxins - toxicity</subject><subject>Base Sequence</subject><subject>bioassays</subject><subject>Biological and medical sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biopesticides</subject><subject>Biotechnology</subject><subject>Cloning, Molecular</subject><subject>Coleoptera - growth & development</subject><subject>Corn</subject><subject>crystal proteins</subject><subject>Diabrotica virgifera virgifera</subject><subject>Endotoxins - chemistry</subject><subject>Endotoxins - genetics</subject><subject>Endotoxins - metabolism</subject><subject>Endotoxins - toxicity</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>genes</topic><topic>Hemolysin Proteins</topic><topic>Hybridization</topic><topic>insect pests</topic><topic>insecticidal properties</topic><topic>Larva - growth & development</topic><topic>larvae</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Mission oriented research</topic><topic>Molecular Sequence Data</topic><topic>molecular weight</topic><topic>nucleotide sequences</topic><topic>Pest Control, Biological</topic><topic>Physiology and Biotechnology</topic><topic>Proteins</topic><topic>Sequence Analysis, DNA</topic><topic>Toxins</topic><topic>Zea mays - parasitology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Baum, J.A</creatorcontrib><creatorcontrib>Chu, C.R</creatorcontrib><creatorcontrib>Rupar, M</creatorcontrib><creatorcontrib>Brown, G.R</creatorcontrib><creatorcontrib>Donovan, W.P</creatorcontrib><creatorcontrib>Huesing, J.E</creatorcontrib><creatorcontrib>Ilagan, O</creatorcontrib><creatorcontrib>Malvar, T.M</creatorcontrib><creatorcontrib>Pleau, M</creatorcontrib><creatorcontrib>Walters, M</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Applied and Environmental Microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Baum, J.A</au><au>Chu, C.R</au><au>Rupar, M</au><au>Brown, G.R</au><au>Donovan, W.P</au><au>Huesing, J.E</au><au>Ilagan, O</au><au>Malvar, T.M</au><au>Pleau, M</au><au>Walters, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binary toxins from Bacillus thuringiensis active against the western corn rootworm, Diabrotica virgifera virgifera LeConte</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>2004-08-01</date><risdate>2004</risdate><volume>70</volume><issue>8</issue><spage>4889</spage><epage>4898</epage><pages>4889-4898</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><coden>AEMIDF</coden><abstract>The western corn rootworm, Diabrotica virgifera virgifera LeConte, is a significant pest of corn in the United States. The development of transgenic corn hybrids resistant to rootworm feeding damage depends on the identification of genes encoding insecticidal proteins toxic to rootworm larvae. In this study, a bioassay screen was used to identify several isolates of the bacterium Bacillus thuringiensis active against rootworm. These bacterial isolates each produce distinct crystal proteins with approximate molecular masses of 13 to 15 kDa and 44 kDa. Insect bioassays demonstrated that both protein classes are required for insecticidal activity against this rootworm species. The genes encoding these proteins are organized in apparent operons and are associated with other genes encoding crystal proteins of unknown function. The antirootworm proteins produced by B. thuringiensis strains EG5899 and EG9444 closely resemble previously described crystal proteins of the Cry34A and Cry35A classes. The antirootworm proteins produced by strain EG4851, designated Cry34Ba1 and Cry35Ba1, represent a new binary toxin. Genes encoding these proteins could become an important component of a sustainable resistance management strategy against this insect pest.</abstract><cop>Washington, DC</cop><pub>American Society for Microbiology</pub><pmid>15294828</pmid><doi>10.1128/AEM.70.8.4889-4898.2004</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence amino acid sequences Animals Bacillus thuringiensis Bacillus thuringiensis - genetics Bacillus thuringiensis - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacterial Proteins - toxicity bacterial toxins Bacterial Toxins - chemistry Bacterial Toxins - genetics Bacterial Toxins - metabolism Bacterial Toxins - toxicity Base Sequence bioassays Biological and medical sciences Biology of microorganisms of confirmed or potential industrial interest Biopesticides Biotechnology Cloning, Molecular Coleoptera - growth & development Corn crystal proteins Diabrotica virgifera virgifera Endotoxins - chemistry Endotoxins - genetics Endotoxins - metabolism Endotoxins - toxicity Fundamental and applied biological sciences. Psychology genes Hemolysin Proteins Hybridization insect pests insecticidal properties Larva - growth & development larvae Microbiology Miscellaneous Mission oriented research Molecular Sequence Data molecular weight nucleotide sequences Pest Control, Biological Physiology and Biotechnology Proteins Sequence Analysis, DNA Toxins Zea mays - parasitology |
title | Binary toxins from Bacillus thuringiensis active against the western corn rootworm, Diabrotica virgifera virgifera LeConte |
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