| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 4557840 | Journal of Invertebrate Pathology | 2013 | 4 Pages |
Vip3Aa, Vip3Ad, Vip3Ae, and Vip3Af proteins from Bacillus thuringiensis were tested for their toxicity against Spodoptera frugiperda and Agrotis ipsilon. Vip3Ad was non-toxic to the two species. Vip3Ae and Vip3Af were significantly more toxic than Vip3Aa against S. frugiperda, both as protoxins and as toxins. Against A. ipsilon, Vip3Ae protoxin was more toxic than Vip3Aa and Vip3Af protoxins. Purification by metal-chelate affinity chromatography significantly affected Vip3Ae toxicity against the two insect species.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The activity of four Vip3A proteins to S. frugiperda and A. ipsilon was tested. ► Vip3Ad was found nontoxic to the two species tested. ► Vip3Ae and Vip3Af were significantly more toxic than Vip3Aa against S. frugiperda. ► Vip3Ae protoxin was more toxic than Vip3Aa and Vip3Af against A. ipsilon. ► Metal-chelate affinity chromatography purification reduced the activity of Vip3Ae.
