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UniProt release 2014_01

Published January 22, 2014


Mouse attacks!

In the arid lands of Arizona lives a fierce predator whose howls pierce the desert night, terrifying its prey. This predator is... a mouse, Onychomys torridus, also called the grasshopper mouse. It may sound like a tale looming straight from the imagination of Tim Burton or Monthy Python, but this mouse really exists. It is carnivorous and it regularly howls just before a kill, although the emitted sound is more a sustained whistle than the actual howl of a wolf. Its prey is no less astonishing, including crickets, other rodents, tarantulas and bark scorpions (Centruroides sculpturatus).

Bark scorpions are not easy prey. They are venomous and inflict intensely painful, sometimes lethal stings. Surprisingly grasshopper mice do not seem to be seriously bothered by that, and it takes little time before the scorpion is captured, killed and eaten. How can O. torridus ignore the venom, while common house mice are sensitive to it? Overall, grasshopper mice do feel pain normally, but when they are injected with scorpion venom or with a physiological saline solution in their hind paws, they are much more irritated by the control saline solution than by the venom. In grasshopper mice, bark scorpion venom acts as an analgesic.

Venom from Buthidae scorpions initiates acute pain in sensitive mammals, such as house mice, rats and humans, by activating the voltage-gated sodium channel Nav1.7/SCN9A, but has no effect on the Nav1.8/SCN10A sodium channel. Recent experiments by Rowe et al. on freshly isolated O. torridus sensory neurons showed that, in this species, the venom strongly inhibits Nav1.8/SCN10A Na+ currents. These Na+ currents are necessary for action potential sustained firing and propagation. By inhibiting Nav1.8/SCN10A, the scorpion venom blocks pain transmission to the central nervous system, and hence induces analgesia. The diametrically opposed response of rodents towards scorpion venom seems to be due to only 2 residues within the Nav1.8/SCN10A sequence. In O. torridus, a glutamate residue is found at position 859 (E-859) and a glutamine residue at position 862 (Q-862), while in species known to be sensitive to the venom, these positions are reversed: Q-859 and E-862. Site-directed mutagenesis of these 2 residues in the O. torridus sequence (Q859E/E862Q) abolished venom sensitivity. Conversely, mutation of the glutamine position in Mus musculus (Q861E) conferred inhibition by C. sculpturatus venom.

Pain sensitivity is essential for survival, since it helps avoid damaging situations. Hence any change in pain perception has to be finely tuned in order not to be deleterious. O. torridus has evolved a brilliant strategy allowing it to exploit an abundant food resource in its environment, i.e. bark scorpions, while keeping intact its ability to feel the necessary pain.

Persistent pain can turn into a nightmare and improving our understanding of pain signaling may be a tremendous help in the discovery of new analgesic drugs. Nav1.7/SCN9A is already under close investigation as a potential target for pain prevention. The new and very exciting study by Rowe et al. shows that the Nav1.8/SCN10A channel also plays a crucial key role in the transmission of pain signals and may be an interesting target for analgesic development.

As of this release, the fully annotated O. torridus Nav1.8/SCN10A protein is available in UniProtKB/Swiss-Prot.

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Modified terms for the feature key ‘Cross-link’ (‘CROSSLNK’ in the flat file):

  • 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain) -> 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-...)
  • 5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain) -> 5'-tyrosyl-5'-aminotyrosine (Tyr-Tyr) (interchain with Y-...)
  • Glycyl threonine ester (Gly-Thr) (interchain with G-...) -> Glycyl threonine ester (Gly-Thr) (interchain with T-...)

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  • Phage maturation
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