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| Author(s): | Bowen D.J., Ensign J.C. |
| Year: | 1998 |
| Title: | Purification and characterization of a high-molecular-weight insecticidal protein complex produced by the entomopathogenic bacterium Photorhabdus luminescens |
| Citation: | Applied and Environmental Microbiology. 64:(8) 3029-3035. . |
Abstract:
When grown in peptone broth, in the absence of nematodes, Photorhabdus luminescens produced a protein toxin complex that was lethal when fed to, or injected into the haemolymph of, Manduca sexta larvae and several other insect species. The toxin was purified as a protein complex with an estimated molecular weight of 1000000 and contained no proteinase, phospholipase, or haemolytic activity and only a trace of lipase activity. The purified toxin possessed insecticidal activity whether injected or given orally. Analyses of the denatured complex by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed it to be composed of several protein subunits ranging in size from 30 to 200 kDa. The complex was further separated by native gel electrophoresis into three components, two of which retained insecticidal activity. The purified native toxin complex was found to be active in nanogram concentrations against M. sexta, Galleria mellonella, Tenebrio molitor, Monomorium pharaonis, Blattella germanica and Periplaneta americana |
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