Tri-trophic effects of transgenic insect-resistant tobacco expressing a protease inhibitor or a biotin-binding protein on adults of the predatory carabid beetle Ctenognathus novaezelandiae
Tri-trophic impacts on adult predatory carabid beetles, Ctenognathus novaezelandiae, of insect-resistant transgenic tobacco plants expressing a serine protease inhibitor, bovine spleen trypsin inhibitor (BSTI), or a biotin-binding protein, avidin, were investigated. Both proteins could potentially a...
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Veröffentlicht in: | Journal of insect physiology 2008-02, Vol.54 (2), p.518-528 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Tri-trophic impacts on adult predatory carabid beetles, Ctenognathus novaezelandiae, of insect-resistant transgenic tobacco plants expressing a serine protease inhibitor, bovine spleen trypsin inhibitor (BSTI), or a biotin-binding protein, avidin, were investigated. Both proteins could potentially affect this beetle, since avidin is known to be insecticidal to many beetle species and C. novaezelandiae midguts were shown to contain high levels of trypsin, a protease powerfully inhibited by bovine pancreatic trypsin inhibitor (a BSTI homologue) in vitro. Newly emerged field-collected adult C. novaezelandiae were fed exclusively for 280 days on Spodoptera litura larvae raised either on non-transgenic control, transgenic avidin (55ppm) or transgenic BSTI (68ppm) tobacco. Despite this long-term exclusive diet, there was no treatment effect on survival or fecundity and only minor and transient effects on beetles were observed. Data pooled across time and genders showed control-prey-fed beetles weighed 3% more than BSTI-prey-fed beetles and avidin-prey-fed beetles consumed 3–4% fewer prey than control- or BSTI-prey-fed individuals. Females in all treatments gained more mass and survived longer than males. Low exposure to the proteins because of dilution and deactivation within the prey is the most likely explanation for the lack of tri-trophic effects observed. Aditionally, the presence of a digestive chymotrypsin only partially inhibited by BSTI may provide an alternative path for proteolysis. |
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ISSN: | 0022-1910 1879-1611 |
DOI: | 10.1016/j.jinsphys.2007.12.002 |