Androctonus australis hector insect toxin

From Wikipedia, the free encyclopedia

Other NamesAaHIT or AaIT
SubtypesAaHIT1, AaHIT2, AaHIT4 and AaHIT5
Latin nameAndroctonus australis hector
English nameSahara scorpion
Androctonus australis hector insect toxin
3D model of AaHIT1 residue 19-88
Names
Other NamesAaHIT or AaIT
SubtypesAaHIT1, AaHIT2, AaHIT4 and AaHIT5
Source
Latin nameAndroctonus australis hector
English nameSahara scorpion
Target
Target channelVoltage-gated sodium channels
Beta-insect excitatory toxin 1
Identifiers
OrganismAndroctonus australis
SymbolAaHIT1
UniProtP01497
Search for
StructuresSwiss-model
DomainsInterPro
Scorpion toxin-like domain
Identifiers
SymbolToxin_3
PfamPF00537
InterProIPR002061
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Androctonus australis hector insect toxin also known as AaHIT is a scorpion toxin which affects voltage-gated sodium channels. Four different insect toxins, namely AaHIT1, AaHIT2, AaHIT4 and AaHIT5, can be distinguished. It targets insects, except AaHIT4, which is also toxic to crustaceans and mammals.[1]

The first three words of Androctonus australis hector insect toxin stem from the Greek words Androctonus and Hector, and the Latin word australis. Androctonus means ‘man-killer’, whereas Hector has the meaning ‘to hold or to possess’ and australis means ‘south’, together constituting ‘the southern man-killer’.

Species distribution

AaHIT can be found in the venom of the North African scorpion, Androctonus australis hector, also known as the Sahara scorpion.

Structure

There are four different forms of AaH insect toxins: AaHIT1, AaHIT2,[2] AaHIT4 [1] and AaHIT5.[3]

The amino acid sequence of AaHIT1 and AaHIT2 only differs at position 17 and 41. The homology between AaHIT4 and AaHIT5 is greater than with the primary structures of AaHIT1 or AaHIT2.

Primary structure of AaHIT1,2,4 and 5

Mode of action

AaHIT specifically affects the voltage-gated sodium channels (VGSC) in insects. The effect of the toxin is excitatory since it shifts the voltage-dependent activation of the sodium channel to lower potentials.[4] This mode of action is comparable to those of beta-toxins. The insect-specific trait most likely derives from the presence of a specific structured loop in the insect VGSCs.[5] In spite of this, some research has shown that AaHIT4 specifically can affect the mammalian sodium channel by modulating alfa- and beta-type anti-mammal neurotoxins binding.[1]

Toxicity

Applications

References

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