Androctonus australis hector insect toxin

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Androctonus australis hector insect toxin
3D model of AaHIT1 residue 19-88
Names
Other Names AaHIT or AaIT
Subtypes AaHIT1, AaHIT2, AaHIT4 and AaHIT5
Source
Latin name Androctonus australis hector
English name Sahara scorpion
Target
Target channel Voltage-gated sodium channels
Beta-insect excitatory toxin 1
Identifiers
Organism Androctonus australis
Symbol AaHIT1
UniProt P01497
Other data
Identifiers
Pfam PF00537
InterPro IPR002061

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]

Etymology[edit]

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[edit]

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

Structure[edit]

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[edit]

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[edit]

The toxin induces muscle contractions of the insects leading to full-body paralysis. Skeletal muscles contract due to the release of excitatory neurotransmitters at the neuromuscular junction. Apart from the AaHIT4 subtype, this effect does not occur in arachnids, crustaceans or mammals.[6]

Applications[edit]

AaHIT seems to be a promising candidate in pest control, e.g. cotton bollworm larvae can be reduced 44-98% by creating transgenic cotton crops which express the AaHIT gene.[7] Another example in which AaHIT can be used as an insecticide is via baculoviruses. Baculoviruses are themselves insect-specific viruses; they can be potentiated if they express the AaHIT gene. The potentiated viruses kill the insects faster, resulting in less damage to the crops.[8]

References[edit]

  1. ^ a b c Loret, EP; Martin-Eauclaire, MF (1991). "An anti-insect toxin purified from the scorpion Androctonus australis Hector also acts on the alpha- and beta-sites of the mammalian sodium channel: sequence and circular dichroism study". Biochemistry 30 (3): 633–40. doi:10.1021/bi00217a007. PMID 1846301. 
  2. ^ Loret, EP; Mansuelle, P (1990). "Neurotoxins Active on Insects: Amino Acid Sequences, Chemical Modifications, and Secondary Structure Estimation by Circular Dichroism of Toxins from the Scorpion Androctonus australis Hector". Biochemistry 29 (6): 1492–501. doi:10.1021/bi00458a021. PMID 2334710. 
  3. ^ Nakagawa, Y; Lee, YM (1997). "Anti-insect toxin 5 (AaIT5) from Androctonus australis". Eur J Biochem 246 (2): 496–501. doi:10.1111/j.1432-1033.1997.t01-1-00496.x. PMID 9208943. 
  4. ^ Lee, D; Adams, ME (2000). "Sodium channels in central neurons of the tobacco budworm, Heliothis virescens: basic properties and modification by scorpion toxins". Journal of Insect Physiology 46 (4): 499–508. doi:10.1016/S0022-1910(99)00136-5. PMID 12770214. 
  5. ^ Shichor, I; Zlotkin, E (2002). "Domain 2 of Drosophila para voltage-gated sodium channel confers insect properties to a rat brain channel". Journal of Neuroscience 22 (11): 4364–71. PMID 12040042. 
  6. ^ Borchani, L; Mansuelle P (1996). "A new scorpion venom toxin paralytic to insects that affects Na+ channel activation. Purification, structure, antigenicity and mode of action". Eur J Biochem 241 (2): 525–32. doi:10.1111/j.1432-1033.1996.00525.x. PMID 8917451. 
  7. ^ Wu, J; Luo, X (1996). "Transgenic cotton expressing synthesized scorpion insect toxin AaHIT gene confers enhanced resistance to cotton bollworm (Heliothis armigera) larvae". Biotechnology Letters 30 (3): 547–54. doi:10.1007/s10529-007-9555-7. PMID 17939056. 
  8. ^ Zlotkin, E; Fishman, Y (2000). "AaIT: from neurotoxin to insecticide". Biochimie 82 (9-10): 869–81. doi:10.1016/S0300-9084(00)01177-9. PMID 11086217.