Insect-active toxins with promiscuous pharmacology from the African theraphosid spider Monocentropus balfouri

Jennifer J. Smith; Volker Herzig; Maria P. Ikonomopoulou; Sławomir Dziemborowicz; Frank Bosmans; Graham M. Nicholson; Glenn F. King

doi:10.3390/toxins9050155

Insect-active toxins with promiscuous pharmacology from the African theraphosid spider Monocentropus balfouri

Jennifer J. Smith, Volker Herzig, Maria P. Ikonomopoulou, Sławomir Dziemborowicz, Frank Bosmans, Graham M. Nicholson, Glenn F. King

School of Medicine

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Many chemical insecticides are becoming less efficacious due to rising resistance in pest species, which has created much interest in the development of new, eco-friendly bioinsecticides. Since insects are the primary prey of most spiders, their venoms are a rich source of insect-active peptides that can be used as leads for new bioinsecticides or as tools to study molecular receptors that are insecticidal targets. In the present study, we isolated two insecticidal peptides, µ/ω-TRTX-Mb1a and -Mb1b, from venom of the African tarantula Monocentropus balfouri. Recombinant µ/ω-TRTX-Mb1a and -Mb1b paralyzed both Lucilia cuprina (Australian sheep blowfly) and Musca domestica (housefly), but neither peptide affected larvae of Helicoverpa armigera (cotton bollworms). Both peptides inhibited currents mediated by voltage-gated sodium (Na_V) and calcium channels in Periplaneta americana (American cockroach) dorsal unpaired median neurons, and they also inhibited the cloned Blattella germanica (German cockroach) Na_V channel (BgNa_V1). An additional effect seen only with Mb1a on BgNa_V1 was a delay in fast inactivation. Comparison of the Na_V channel sequences of the tested insect species revealed that variations in the S1–S2 loops in the voltage sensor domains might underlie the differences in activity between different phyla.

Original language	English (US)
Article number	155
Journal	Toxins
Volume	9
Issue number	5
DOIs	https://doi.org/10.3390/toxins9050155
State	Published - May 2017

Keywords

Calcium channel
Insecticide
Pharmacology
Sodium channel
Spider
Venom

ASJC Scopus subject areas

Toxicology
Health, Toxicology and Mutagenesis

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10.3390/toxins9050155

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title = "Insect-active toxins with promiscuous pharmacology from the African theraphosid spider Monocentropus balfouri",

abstract = "Many chemical insecticides are becoming less efficacious due to rising resistance in pest species, which has created much interest in the development of new, eco-friendly bioinsecticides. Since insects are the primary prey of most spiders, their venoms are a rich source of insect-active peptides that can be used as leads for new bioinsecticides or as tools to study molecular receptors that are insecticidal targets. In the present study, we isolated two insecticidal peptides, µ/ω-TRTX-Mb1a and -Mb1b, from venom of the African tarantula Monocentropus balfouri. Recombinant µ/ω-TRTX-Mb1a and -Mb1b paralyzed both Lucilia cuprina (Australian sheep blowfly) and Musca domestica (housefly), but neither peptide affected larvae of Helicoverpa armigera (cotton bollworms). Both peptides inhibited currents mediated by voltage-gated sodium (NaV) and calcium channels in Periplaneta americana (American cockroach) dorsal unpaired median neurons, and they also inhibited the cloned Blattella germanica (German cockroach) NaV channel (BgNaV1). An additional effect seen only with Mb1a on BgNaV1 was a delay in fast inactivation. Comparison of the NaV channel sequences of the tested insect species revealed that variations in the S1–S2 loops in the voltage sensor domains might underlie the differences in activity between different phyla.",

keywords = "Calcium channel, Insecticide, Pharmacology, Sodium channel, Spider, Venom",

author = "Smith, {Jennifer J.} and Volker Herzig and Ikonomopoulou, {Maria P.} and S{\l}awomir Dziemborowicz and Frank Bosmans and Nicholson, {Graham M.} and King, {Glenn F.}",

note = "Funding Information: The authors thank the Australian Grains Research & Development Corporation (GRDC; Project UQ00048, Kingston, Australia) for financial support, Arnd Schlosser (Bremen, Germany) for venom extraction, Michael Scheller (Mainz, Germany) for providing the spider, Geoff Brown (Department of Agriculture, Fisheries and Forestry, Brisbane, Australia) for supply of blowflies, and Ke Dong (Michigan State University, East Lansing, MI, USA) for sharing the BgNaV1/TipE clones. This research was facilitated by access to the Australian Proteome Analysis Facility (Sydney, Australia), which is supported under the Australian Government{\textquoteright}s National Collaborative Research Infrastructure Strategy. G.F.K. is supported by a Principal Research Fellowship (APP1044414) from the Australian National Health & Medical Research Council (Canberra, Australia). Publisher Copyright: {\textcopyright} 2017 by the authors. Licensee MDPI, Basel, Switzerland.",

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doi = "10.3390/toxins9050155",

language = "English (US)",

volume = "9",

journal = "Toxins",

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AU - Smith, Jennifer J.

AU - Herzig, Volker

AU - Ikonomopoulou, Maria P.

AU - Dziemborowicz, Sławomir

AU - Bosmans, Frank

AU - Nicholson, Graham M.

AU - King, Glenn F.

N1 - Funding Information: The authors thank the Australian Grains Research & Development Corporation (GRDC; Project UQ00048, Kingston, Australia) for financial support, Arnd Schlosser (Bremen, Germany) for venom extraction, Michael Scheller (Mainz, Germany) for providing the spider, Geoff Brown (Department of Agriculture, Fisheries and Forestry, Brisbane, Australia) for supply of blowflies, and Ke Dong (Michigan State University, East Lansing, MI, USA) for sharing the BgNaV1/TipE clones. This research was facilitated by access to the Australian Proteome Analysis Facility (Sydney, Australia), which is supported under the Australian Government’s National Collaborative Research Infrastructure Strategy. G.F.K. is supported by a Principal Research Fellowship (APP1044414) from the Australian National Health & Medical Research Council (Canberra, Australia). Publisher Copyright: © 2017 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2017/5

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N2 - Many chemical insecticides are becoming less efficacious due to rising resistance in pest species, which has created much interest in the development of new, eco-friendly bioinsecticides. Since insects are the primary prey of most spiders, their venoms are a rich source of insect-active peptides that can be used as leads for new bioinsecticides or as tools to study molecular receptors that are insecticidal targets. In the present study, we isolated two insecticidal peptides, µ/ω-TRTX-Mb1a and -Mb1b, from venom of the African tarantula Monocentropus balfouri. Recombinant µ/ω-TRTX-Mb1a and -Mb1b paralyzed both Lucilia cuprina (Australian sheep blowfly) and Musca domestica (housefly), but neither peptide affected larvae of Helicoverpa armigera (cotton bollworms). Both peptides inhibited currents mediated by voltage-gated sodium (NaV) and calcium channels in Periplaneta americana (American cockroach) dorsal unpaired median neurons, and they also inhibited the cloned Blattella germanica (German cockroach) NaV channel (BgNaV1). An additional effect seen only with Mb1a on BgNaV1 was a delay in fast inactivation. Comparison of the NaV channel sequences of the tested insect species revealed that variations in the S1–S2 loops in the voltage sensor domains might underlie the differences in activity between different phyla.

AB - Many chemical insecticides are becoming less efficacious due to rising resistance in pest species, which has created much interest in the development of new, eco-friendly bioinsecticides. Since insects are the primary prey of most spiders, their venoms are a rich source of insect-active peptides that can be used as leads for new bioinsecticides or as tools to study molecular receptors that are insecticidal targets. In the present study, we isolated two insecticidal peptides, µ/ω-TRTX-Mb1a and -Mb1b, from venom of the African tarantula Monocentropus balfouri. Recombinant µ/ω-TRTX-Mb1a and -Mb1b paralyzed both Lucilia cuprina (Australian sheep blowfly) and Musca domestica (housefly), but neither peptide affected larvae of Helicoverpa armigera (cotton bollworms). Both peptides inhibited currents mediated by voltage-gated sodium (NaV) and calcium channels in Periplaneta americana (American cockroach) dorsal unpaired median neurons, and they also inhibited the cloned Blattella germanica (German cockroach) NaV channel (BgNaV1). An additional effect seen only with Mb1a on BgNaV1 was a delay in fast inactivation. Comparison of the NaV channel sequences of the tested insect species revealed that variations in the S1–S2 loops in the voltage sensor domains might underlie the differences in activity between different phyla.

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KW - Pharmacology

KW - Sodium channel

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Insect-active toxins with promiscuous pharmacology from the African theraphosid spider Monocentropus balfouri

Abstract

Keywords

ASJC Scopus subject areas

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