Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.

Many insect pests have developed resistance to existing chemical insecticides and consequently there is much interest in the development of new insecticidal compounds with novel modes of action. Although spiders have deployed insecticidal toxins in their venoms for over 250 million years, there is n...

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Autores principales:	Margaret C Hardy, Norelle L Daly, Mehdi Mobli, Rodrigo A V Morales, Glenn F King
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/eaa90503fd204018bedc2c0058e75502
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spelling	oai:doaj.org-article:eaa90503fd204018bedc2c0058e755022021-11-18T08:55:49ZIsolation of an orally active insecticidal toxin from the venom of an Australian tarantula.1932-620310.1371/journal.pone.0073136https://doaj.org/article/eaa90503fd204018bedc2c0058e755022013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24039872/?tool=EBIhttps://doaj.org/toc/1932-6203Many insect pests have developed resistance to existing chemical insecticides and consequently there is much interest in the development of new insecticidal compounds with novel modes of action. Although spiders have deployed insecticidal toxins in their venoms for over 250 million years, there is no evolutionary selection pressure on these toxins to possess oral activity since they are injected into prey and predators via a hypodermic needle-like fang. Thus, it has been assumed that spider-venom peptides are not orally active and are therefore unlikely to be useful insecticides. Contrary to this dogma, we show that it is possible to isolate spider-venom peptides with high levels of oral insecticidal activity by directly screening for per os toxicity. Using this approach, 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.Margaret C HardyNorelle L DalyMehdi MobliRodrigo A V MoralesGlenn F KingPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e73136 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Margaret C Hardy Norelle L Daly Mehdi Mobli Rodrigo A V Morales Glenn F King Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.
description	Many insect pests have developed resistance to existing chemical insecticides and consequently there is much interest in the development of new insecticidal compounds with novel modes of action. Although spiders have deployed insecticidal toxins in their venoms for over 250 million years, there is no evolutionary selection pressure on these toxins to possess oral activity since they are injected into prey and predators via a hypodermic needle-like fang. Thus, it has been assumed that spider-venom peptides are not orally active and are therefore unlikely to be useful insecticides. Contrary to this dogma, we show that it is possible to isolate spider-venom peptides with high levels of oral insecticidal activity by directly screening for per os toxicity. Using this approach, 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.
format	article
author	Margaret C Hardy Norelle L Daly Mehdi Mobli Rodrigo A V Morales Glenn F King
author_facet	Margaret C Hardy Norelle L Daly Mehdi Mobli Rodrigo A V Morales Glenn F King
author_sort	Margaret C Hardy
title	Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.
title_short	Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.
title_full	Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.
title_fullStr	Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.
title_full_unstemmed	Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.
title_sort	isolation of an orally active insecticidal toxin from the venom of an australian tarantula.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/eaa90503fd204018bedc2c0058e75502
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Isolation of an orally active insecticidal toxin from the venom of an Australian tarantula.

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