Activity of Bacillus thuringiensis hybrid protein against a lepidopteran and a coleopteran pest
Abstract The use of Cry proteins from Bacillus thuringiensis are an important strategy for biological control. Recently it has been demonstrated that Cry hybrid proteins (by domain swapping) resulted in improved toxicities in comparison with parental proteins. Here, an SN1917 hybrid toxin was constr...
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| Veröffentlicht in: | FEMS microbiology letters 2010-01, Vol.302 (2), p.93-98 |
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| creator | López-Pazos, Silvio Alejandro Rojas Arias, Adriana Carolina Ospina, Sonia A. Cerón, Jairo |
| description | Abstract
The use of Cry proteins from Bacillus thuringiensis are an important strategy for biological control. Recently it has been demonstrated that Cry hybrid proteins (by domain swapping) resulted in improved toxicities in comparison with parental proteins. Here, an SN1917 hybrid toxin was constructed and tested against Colombian pest insects Tecia solanivora (Lepidoptera: Gelechiidae), a severe potato pest, and Hypothenemus hampei (Coleoptera: Scolytidae), which attacks coffee crops. The SN1917 protoxin had a concentration causing 50% mortality (LC50) of 392 ng cm–2, and SN1917 toxin showed an LC50 of 201 ng cm–2 against T. solanivora first instar larvae. The two parental toxins (Cry1B and Cry1I) used to make this new hybrid protein caused a mortality of 60% and 52%, respectively. Unfortunately, H. hampei first instar larvae proved to be resistant to the toxin. We conclude that SN1917 is an option for biological control and resistance management of T. solanivora. Implications for H. hampei are discussed. |
| doi_str_mv | 10.1111/j.1574-6968.2009.01821.x |
| format | Article |
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The use of Cry proteins from Bacillus thuringiensis are an important strategy for biological control. Recently it has been demonstrated that Cry hybrid proteins (by domain swapping) resulted in improved toxicities in comparison with parental proteins. Here, an SN1917 hybrid toxin was constructed and tested against Colombian pest insects Tecia solanivora (Lepidoptera: Gelechiidae), a severe potato pest, and Hypothenemus hampei (Coleoptera: Scolytidae), which attacks coffee crops. The SN1917 protoxin had a concentration causing 50% mortality (LC50) of 392 ng cm–2, and SN1917 toxin showed an LC50 of 201 ng cm–2 against T. solanivora first instar larvae. The two parental toxins (Cry1B and Cry1I) used to make this new hybrid protein caused a mortality of 60% and 52%, respectively. Unfortunately, H. hampei first instar larvae proved to be resistant to the toxin. We conclude that SN1917 is an option for biological control and resistance management of T. solanivora. Implications for H. hampei are discussed.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2009.01821.x</identifier><identifier>PMID: 20002185</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Bacillus thuringiensis ; Bacillus thuringiensis - genetics ; Bacterial Toxins - genetics ; Bacterial Toxins - pharmacology ; Bacteriology ; Biological and medical sciences ; Biological control ; Coffee ; Coleoptera - drug effects ; Fundamental and applied biological sciences. Psychology ; hybrid Cry protein ; Hypothenemus hampei ; Insecticides - pharmacology ; Insects ; Larva - drug effects ; Larvae ; Lepidoptera - drug effects ; Lethal Dose 50 ; Microbiology ; Miscellaneous ; Molecular Sequence Data ; Mortality ; Pest resistance ; Pests ; Potatoes ; Proteins ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - pharmacology ; Sequence Alignment ; Survival Analysis ; Tecia solanivora ; Toxins</subject><ispartof>FEMS microbiology letters, 2010-01, Vol.302 (2), p.93-98</ispartof><rights>2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2009</rights><rights>2009 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2009.01821.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2009.01821.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,4009,27902,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22238982$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20002185$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>López-Pazos, Silvio Alejandro</creatorcontrib><creatorcontrib>Rojas Arias, Adriana Carolina</creatorcontrib><creatorcontrib>Ospina, Sonia A.</creatorcontrib><creatorcontrib>Cerón, Jairo</creatorcontrib><title>Activity of Bacillus thuringiensis hybrid protein against a lepidopteran and a coleopteran pest</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The use of Cry proteins from Bacillus thuringiensis are an important strategy for biological control. Recently it has been demonstrated that Cry hybrid proteins (by domain swapping) resulted in improved toxicities in comparison with parental proteins. Here, an SN1917 hybrid toxin was constructed and tested against Colombian pest insects Tecia solanivora (Lepidoptera: Gelechiidae), a severe potato pest, and Hypothenemus hampei (Coleoptera: Scolytidae), which attacks coffee crops. The SN1917 protoxin had a concentration causing 50% mortality (LC50) of 392 ng cm–2, and SN1917 toxin showed an LC50 of 201 ng cm–2 against T. solanivora first instar larvae. The two parental toxins (Cry1B and Cry1I) used to make this new hybrid protein caused a mortality of 60% and 52%, respectively. Unfortunately, H. hampei first instar larvae proved to be resistant to the toxin. We conclude that SN1917 is an option for biological control and resistance management of T. solanivora. Implications for H. hampei are discussed.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - genetics</subject><subject>Bacterial Toxins - genetics</subject><subject>Bacterial Toxins - pharmacology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biological control</subject><subject>Coffee</subject><subject>Coleoptera - drug effects</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hybrid Cry protein</subject><subject>Hypothenemus hampei</subject><subject>Insecticides - pharmacology</subject><subject>Insects</subject><subject>Larva - drug effects</subject><subject>Larvae</subject><subject>Lepidoptera - drug effects</subject><subject>Lethal Dose 50</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Mortality</subject><subject>Pest resistance</subject><subject>Pests</subject><subject>Potatoes</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - pharmacology</subject><subject>Sequence Alignment</subject><subject>Survival Analysis</subject><subject>Tecia solanivora</subject><subject>Toxins</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kU1v1DAQhi0EokvhLyBLCG4JM-N8OAcOpaKAtIgLnC0nmbReeZMQJ6X773HYbZFA-GJr5nnnw68QEiHFeN7uUszLLCmqQqcEUKWAmjC9eyQ2D4nHYgOq1AlCVZ6JZyHsACAjKJ6Ks6gBQp1vhLloZnfr5oMcOvneNs77Jcj5Zplcf-24Dy7Im0M9uVaO0zCz66W9tq4Ps7TS8-jaYZx5sjHctzHUDJ7vIyOH-bl40lkf-MXpPhffrz58u_yUbL9-_Hx5sU0GVZWY5MRZm9cKQGW6gkZ3WhVokUBzSRprQMaaqCu5BlYdtIQZcV012CJ3pToXb45145Q_ltjY7F1o2Hvb87AEQ0iaiiqP4Ku_wN2wTH2czZCCgmJ7pEi9PFFLvefWjJPb2-lg7j8uAq9PgA2N9V3ct3HhD0ekdKXXQu-O3E_n-fCQRzCrkWZnVr_M6tdauzK_jTR35urLdn1FvTrqh2X8jzr5R61-AVQDnx8</recordid><startdate>20100101</startdate><enddate>20100101</enddate><creator>López-Pazos, Silvio Alejandro</creator><creator>Rojas Arias, Adriana Carolina</creator><creator>Ospina, Sonia A.</creator><creator>Cerón, Jairo</creator><general>Blackwell Publishing Ltd</general><general>Wiley-Blackwell</general><general>Oxford University Press</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7SS</scope><scope>7ST</scope><scope>SOI</scope></search><sort><creationdate>20100101</creationdate><title>Activity of Bacillus thuringiensis hybrid protein against a lepidopteran and a coleopteran pest</title><author>López-Pazos, Silvio Alejandro ; Rojas Arias, Adriana Carolina ; Ospina, Sonia A. ; Cerón, Jairo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-o3971-52e4d5b30034890c8f8361a1208e7281b01e1b22f7eb0e3f0d2142eb9c1d1ef73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacillus thuringiensis</topic><topic>Bacillus thuringiensis - genetics</topic><topic>Bacterial Toxins - genetics</topic><topic>Bacterial Toxins - pharmacology</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Biological control</topic><topic>Coffee</topic><topic>Coleoptera - drug effects</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hybrid Cry protein</topic><topic>Hypothenemus hampei</topic><topic>Insecticides - pharmacology</topic><topic>Insects</topic><topic>Larva - drug effects</topic><topic>Larvae</topic><topic>Lepidoptera - drug effects</topic><topic>Lethal Dose 50</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Mortality</topic><topic>Pest resistance</topic><topic>Pests</topic><topic>Potatoes</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - pharmacology</topic><topic>Sequence Alignment</topic><topic>Survival Analysis</topic><topic>Tecia solanivora</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>López-Pazos, Silvio Alejandro</creatorcontrib><creatorcontrib>Rojas Arias, Adriana Carolina</creatorcontrib><creatorcontrib>Ospina, Sonia A.</creatorcontrib><creatorcontrib>Cerón, Jairo</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Environment Abstracts</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>López-Pazos, Silvio Alejandro</au><au>Rojas Arias, Adriana Carolina</au><au>Ospina, Sonia A.</au><au>Cerón, Jairo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activity of Bacillus thuringiensis hybrid protein against a lepidopteran and a coleopteran pest</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2010-01-01</date><risdate>2010</risdate><volume>302</volume><issue>2</issue><spage>93</spage><epage>98</epage><pages>93-98</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>Abstract
The use of Cry proteins from Bacillus thuringiensis are an important strategy for biological control. Recently it has been demonstrated that Cry hybrid proteins (by domain swapping) resulted in improved toxicities in comparison with parental proteins. Here, an SN1917 hybrid toxin was constructed and tested against Colombian pest insects Tecia solanivora (Lepidoptera: Gelechiidae), a severe potato pest, and Hypothenemus hampei (Coleoptera: Scolytidae), which attacks coffee crops. The SN1917 protoxin had a concentration causing 50% mortality (LC50) of 392 ng cm–2, and SN1917 toxin showed an LC50 of 201 ng cm–2 against T. solanivora first instar larvae. The two parental toxins (Cry1B and Cry1I) used to make this new hybrid protein caused a mortality of 60% and 52%, respectively. Unfortunately, H. hampei first instar larvae proved to be resistant to the toxin. We conclude that SN1917 is an option for biological control and resistance management of T. solanivora. Implications for H. hampei are discussed.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>20002185</pmid><doi>10.1111/j.1574-6968.2009.01821.x</doi><tpages>6</tpages></addata></record> |
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| ispartof | FEMS microbiology letters, 2010-01, Vol.302 (2), p.93-98 |
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| subjects | Amino Acid Sequence Animals Bacillus thuringiensis Bacillus thuringiensis - genetics Bacterial Toxins - genetics Bacterial Toxins - pharmacology Bacteriology Biological and medical sciences Biological control Coffee Coleoptera - drug effects Fundamental and applied biological sciences. Psychology hybrid Cry protein Hypothenemus hampei Insecticides - pharmacology Insects Larva - drug effects Larvae Lepidoptera - drug effects Lethal Dose 50 Microbiology Miscellaneous Molecular Sequence Data Mortality Pest resistance Pests Potatoes Proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - pharmacology Sequence Alignment Survival Analysis Tecia solanivora Toxins |
| title | Activity of Bacillus thuringiensis hybrid protein against a lepidopteran and a coleopteran pest |
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