Source:http://linkedlifedata.com/resource/pubmed/id/13678710
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2003-9-18
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pubmed:abstractText |
Baculovirus occlusion bodies, large proteinaceous structures which contain virions, have recently been engineered to incorporate foreign proteins. The major constituent protein of occlusion bodies from the baculovirus Autographa californica nucleopolyhedrovirus is polyhedrin, and assembly of recombinant occlusion bodies which incorporate a foreign protein depends on an interaction between native polyhedrin and a polyhedrin-foreign protein fusion. This technology has now been applied to the generation of a recombinant baculovirus (ColorBtrus) that produces occlusion bodies incorporating the Bacillus thuringiensis (Bt) insecticidal Cry1Ac toxin protein. ColorBtrus coexpresses native polyhedrin and a fusion protein in which polyhedrin is fused to the Bt toxin, which is in turn fused to green fluorescent protein (GFP). Analysis of ColorBtrus occlusion bodies confirmed that they include both Bt toxin and GFP, yet still incorporate virions. Bioassay of ColorBtrus demonstrated that its speed of action and pathogenicity are strikingly enhanced compared to wild-type virus. ColorBtrus represents a novel, powerful biological insecticide that combines positive attributes of both Bt toxin and baculovirus based systems.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Structural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/polyhedrin protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0022-2011
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:13678710-Animals,
pubmed-meshheading:13678710-Base Sequence,
pubmed-meshheading:13678710-Endotoxins,
pubmed-meshheading:13678710-Genetic Vectors,
pubmed-meshheading:13678710-Green Fluorescent Proteins,
pubmed-meshheading:13678710-Immunoblotting,
pubmed-meshheading:13678710-Immunohistochemistry,
pubmed-meshheading:13678710-Inclusion Bodies,
pubmed-meshheading:13678710-Luminescent Proteins,
pubmed-meshheading:13678710-Nucleopolyhedrovirus,
pubmed-meshheading:13678710-Pest Control, Biological,
pubmed-meshheading:13678710-Recombinant Fusion Proteins,
pubmed-meshheading:13678710-Viral Proteins,
pubmed-meshheading:13678710-Viral Structural Proteins,
pubmed-meshheading:13678710-Virulence
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pubmed:year |
2003
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pubmed:articleTitle |
An improved baculovirus insecticide producing occlusion bodies that contain Bacillus thuringiensis insect toxin.
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pubmed:affiliation |
School of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University, Suwon 441-744, Republic of Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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