Bioaccumulation of Cry1Ab protein from an herbivore reduces anti-oxidant enzyme activities in two spider species.
Cry proteins are expressed in rice lines for lepidopteran pest control. These proteins can be transferred from transgenic rice plants to non-target arthropods, including planthoppers and then to a predatory spider. Movement of Cry proteins through food webs may reduce fitness of non-target arthropods, although recent publications indicated no serious changes in non-target populations. Nonetheless, Cry protein intoxication influences gene expression in Cry-sensitive insects. We posed the hypothesis that Cry protein intoxication influences enzyme activities in spiders acting in tri-trophic food webs. Here we report on the outcomes of experiments designed to test our hypothesis with two spider species. We demonstrated that the movement of CryAb protein from Drosophila culture medium into fruit flies maintained on the CryAb containing medium and from the flies to the spiders Ummeliata insecticeps and Pardosa pseudoannulata. We also show that the activities of three key metabolic enzymes, acetylcholine esterase (AchE), glutathione peroxidase (GSH-Px), and superoxide dismutase (SOD) were significantly influenced in the spiders after feeding on Cry1Ab-containing fruit flies. We infer from these data that Cry proteins originating in transgenic crops impacts non-target arthropods at the physiological and biochemical levels, which may be one mechanism of Cry protein-related reductions in fitness of non-target beneficial predators.
College of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Ji
J
Zhou
College of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Kaifu
K
Xiao
College of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Baoyang
B
Wei
College of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Zhi
Z
Wang
College of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Yun
Y
Tian
College of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China.
Yixing
Y
Tian
College of Bioscience & Biotechnology, Hunan Agriculture University, Changsha, China ; Division of Plant Sciences, University of Missouri, Columbia, Missouri, United States of America.
Qisheng
Q
Song
D000110:Acetylcholinesterase / Q000378:metabolism; D000818:Animals; D000975:Antioxidants / Q000378:metabolism*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000378:metabolism*; D003470:Culture Media; D004331:Drosophila melanogaster / Q000378:metabolism*; D004731:Endotoxins / Q000378:metabolism*; D005979:Glutathione Peroxidase / Q000378:metabolism; D006460:Hemolysin Proteins / Q000378:metabolism*; D060434:Herbivory / Q000502:physiology*; D013112:Spiders / Q000201:enzymology*; D013482:Superoxide Dismutase / Q000378:metabolism
D000975:Antioxidants; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D003470:Culture Media; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D000110:Acetylcholinesterase