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Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula (Table S1)

The University of Queensland
Adjunct Professor Norelle Daly (Aggregated by) Associate Professor Mehdi Mobli (Aggregated by) Dr Maggie Hardy (Aggregated by) Dr Maggie Hardy (Aggregated by) Dr Rodrigo Morales (Aggregated by)
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ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Adc&rfr_id=info%3Asid%2FANDS&rft_id=info:doi10.1371/journal.pone.0073136.s001&rft.title=Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula (Table S1)&rft.identifier=10.1371/journal.pone.0073136.s001&rft.publisher=The University of Queensland&rft.description=We isolated a 34-residue orally active insecticidal peptide (OAIP-1) from venom of the Australian tarantula Selenotypus plumipes. The oral LD50 for OAIP-1 in the agronomically important cotton bollworm Helicoverpa armigera was 104.2±0.6 pmol/g, which is the highest per os activity reported to date for an insecticidal venom peptide. OAIP-1 is equipotent with synthetic pyrethroids and it acts synergistically with neonicotinoid insecticides. The three-dimensional structure of OAIP-1 determined using NMR spectroscopy revealed that the three disulfide bonds form an inhibitor cystine knot motif; this structural motif provides the peptide with a high level of biological stability that probably contributes to its oral activity. OAIP-1 is likely to be synergized by the gut-lytic activity of the Bacillus thuringiensis Cry toxin (Bt) expressed in insect-resistant transgenic crops, and consequently it might be a good candidate for trait stacking with Bt.&rft.creator=Adjunct Professor Norelle Daly&rft.creator=Associate Professor Mehdi Mobli&rft.creator=Dr Maggie Hardy&rft.creator=Dr Maggie Hardy&rft.creator=Dr Rodrigo Morales&rft.creator=Professor Glenn King&rft.creator=Professor Glenn King&rft.creator=Professor Mehdi Mobli&rft.date=2013&rft_rights=2013, The University of Queensland&rft_rights= http://creativecommons.org/licenses/by/3.0/deed.en_US&rft_subject=eng&rft_subject=Toxins&rft_subject=Venoms&rft_subject=Orally active toxins&rft_subject=Insecticides&rft_subject=Spiders&rft_subject=Australian spiders&rft_subject=BIOLOGICAL SCIENCES&rft.type=dataset&rft.language=English Access the data
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2013, The University of Queensland

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We isolated a 34-residue orally active insecticidal peptide (OAIP-1) from venom of the Australian tarantula Selenotypus plumipes. The oral LD50 for OAIP-1 in the agronomically important cotton bollworm Helicoverpa armigera was 104.2±0.6 pmol/g, which is the highest per os activity reported to date for an insecticidal venom peptide. OAIP-1 is equipotent with synthetic pyrethroids and it acts synergistically with neonicotinoid insecticides. The three-dimensional structure of OAIP-1 determined using NMR spectroscopy revealed that the three disulfide bonds form an inhibitor cystine knot motif; this structural motif provides the peptide with a high level of biological stability that probably contributes to its oral activity. OAIP-1 is likely to be synergized by the gut-lytic activity of the Bacillus thuringiensis Cry toxin (Bt) expressed in insect-resistant transgenic crops, and consequently it might be a good candidate for trait stacking with Bt.

Issued: 2013

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Subjects
Australian spiders | Biological Sciences | Insecticides | Orally active toxins | Spiders | Toxins | Venoms | eng |

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