Recombinant Leiurus quinquestriatus Alpha-insect toxin LqhaIT protein (His tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Alpha-insect toxin LqhaIT also known as Leiurus quinquestriatus toxin is a neurotoxic peptide expressed by the venom of the scorpion Leiurus quinquestriatus. This toxin has a molecular mass of approximately 7 kDa. Alpha-insect toxin LqhaIT targets insect sodium channels by binding specifically to voltage-gated sodium channels altering their normal function. This binding causes prolonged channel opening disrupting the normal electrical signals in nerve cells ultimately leading to paralysis of insects.

Biological function summary

Alpha-insect toxin LqhaIT serves as a potent insecticidal agent without forming part of a larger protein complex. The toxin's specific interaction with insect voltage-gated sodium channels makes it an important factor in the scorpion's venom lethality. These interactions primarily impact the nervous system of insects leading to their incapacitation. This specificity highlights evolutionary adaptations between predators and prey resulting in a highly specialized mechanism for subduing insect prey.

Pathways

Alpha-insect toxin LqhaIT's action integrates into the pathways that explore ion channel function and neurotoxicity. It affects pathways involving the regulation of neuronal excitability due to its ability to modulate sodium channels similar to other neurotoxins. Its effects resemble those of other voltage-gated sodium channel modifiers like tetrodotoxin and saxitoxin which are known for their roles in the nervous system as channel blockers. By interfering with these pathways Alpha-insect toxin LqhaIT provides insights into the workings of neurotoxic agents.

Alpha-insect toxin LqhaIT holds potential relevance to certain neurological conditions although it primarily affects insects. Its modulation of sodium channels shares similarities with mechanisms observed in disorders such as epilepsy where sodium channel dysfunction can play a role. Furthermore the study of this toxin could lead to a better understanding of sodium channelopathies conditions where abnormal sodium channel function disrupts normal cellular activities. By comparing its action to human sodium channel-related disorders scientists can explore therapeutic possibilities and gain a better understanding of similar neurotoxins like brevetoxins which affect marine life and humans.