Proteomics

Dataset Information

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Peptide toxins that target vertebrate voltage-gated sodium channels underly the painful stings of harvester ants


ABSTRACT: Harvester ants (genus Pogonomyrmex) are notable for their stings which cause intense, long-lasting pain and other neurotoxic symptoms in vertebrates. Here we show that harvester ant venoms are relatively simple and composed largely of peptide toxins. One class of peptides is primarily responsible for the long-lasting local pain of envenomation. These hydrophobic, cysteine-free peptides activate mammalian sensory neurons via potent modulation of voltage-gated sodium (NaV) channels, reducing voltage threshold for activation and inhibiting channel inactivation. These toxins appear to have evolved specifically as deterrents against vertebrates.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Pogonomyrmex

TISSUE(S): Venom

SUBMITTER: Vanessa Schendel  

LAB HEAD: Samuel D. Robinson

PROVIDER: PXD043773 | Pride | 2024-06-16

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
SR_20190731_Pmaricopa_VR.group Other
SR_20190731_Pmaricopa_VR.wiff Wiff
SR_20190731_Pmaricopa_VR.wiff.scan Wiff
SR_20190731_Pmaricopa_VR_RA.group Other
SR_20190731_Pmaricopa_VR_RA.wiff Wiff
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Publications

Peptide toxins that target vertebrate voltage-gated sodium channels underly the painful stings of harvester ants.

Robinson Samuel D SD   Deuis Jennifer R JR   Niu Pancong P   Touchard Axel A   Mueller Alexander A   Schendel Vanessa V   Brinkwirth Nina N   King Glenn F GF   Vetter Irina I   Schmidt Justin O JO  

The Journal of biological chemistry 20231216 1


Harvester ants (genus Pogonomyrmex) are renowned for their stings which cause intense, long-lasting pain, and other neurotoxic symptoms in vertebrates. Here, we show that harvester ant venoms are relatively simple and composed largely of peptide toxins. One class of peptides is primarily responsible for the long-lasting local pain of envenomation via activation of peripheral sensory neurons. These hydrophobic, cysteine-free peptides potently modulate mammalian voltage-gated sodium (Na<sub>V</sub  ...[more]

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