Delta endotoxins

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Delta endotoxin, N-terminal domain
TCDB
1.C.2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Delta endotoxin, middle domain
Identifiers
SymbolEndotoxin_M
TCDB
1.C.2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Delta endotoxin, C-terminal
Identifiers
SymbolEndotoxin_C
TCDB
1.C.2
CDDcd04085
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cytolytic delta-endotoxin Cyt1/2
Identifiers
SymbolCytB
TCDB
1.C.71
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Delta endotoxins (δ-endotoxins) are a family of

Bt maize/corn and other GM crops. During spore formation the bacteria produce crystals of such proteins (hence the name Cry toxins) that are also known as parasporal bodies, next to the endospores; as a result some members are known as a parasporin. The Cyt (cytolytic) toxin group is another group of delta-endotoxins formed in the cytoplasm. VIP toxins (vegetative insecticidal proteins) are formed at other stages of the life cycle.[2]

Mechanism of action

When an insect ingests these proteins, they are activated by proteolytic cleavage. The N-terminus is cleaved in all of the proteins and a C-terminal extension is cleaved in some members. Once activated, the endotoxin binds to the gut

cell lysis by the formation of cation-selective channels, which leads to death.[3][1]

For many years there was no clarity as to the relationship between

Trichoplusia ni by Baxter et al. 2011 and Tiewsiri & Wang 2011 (also all Lepidoptera).[7] There continues to be confirmation that AP-Ns do not by themselves affect resistance in some cases, possibly due to sequential binding by the toxin being required to produce its effect. In this sequence each binding step is theoretically not indispensable, but if it occurs does contribute to the final pore formation result.[8]

Structure

The activated region of the delta toxin is composed of three distinct

beta-sheet central domain involved in receptor binding; and a C-terminal beta-sandwich domain (InterProIPR005638) that interacts with the N-terminal domain to form a channel.[1][3]

Types

B. thuringiensis encodes many proteins of the delta endotoxin family (InterProIPR038979), with some strains encoding multiple types simultaneously.[9] A gene mostly found on plasmids,[10] delta-entotoxins sometimes show up in genomes of other species, albeit at a lower proportion than those found in B. thuringiensis.[11] The gene names looks like Cry3Bb, which in this case indicates a Cry toxin of superfamily 3 family B subfamily b.[12]

Cry proteins that are interesting to cancer research are listed under a parasporin (PS) nomenclature in addition to the Cry nomenclature. They do not kill insects, but instead kill leukemia cells.[13][14][15] The Cyt toxins tend to form their own group distinct from Cry toxins.[16] Not all Cry — crystal-form — toxins directly share a common root.[17] Examples of non-three-domain toxins that nevertheless have a Cry name include Cry34/35Ab1 and related beta-sandwich binary (Bin-like) toxins, Cry6Aa, and many beta-sandwich parasporins.[18]

Specific delta-endotoxins that have been inserted with

maize/corn.[19] In addition, Cry1Ac is effective as a vaccine adjuvant in humans.[20]

Some insects populations have started to develop resistance towards delta endotoxin, with five resistant species found as of 2013. Plants with two kinds of delta endotoxins tend to make resistance happen slower, as the insects have to evolve to overcome both toxins at once. Planting non-Bt plants with the resistant plants will reduce the selection pressure for developing the toxin. Finally, two-toxin plants should not be planted with one-toxin plants, as one-toxin plants act as a stepping stone for adaption in this case.[19]

References

  1. ^
    PMID 11468393
    .
  2. ^ Roger Hull; et al. (2021). "Risk assessment and management—Environment". Genetically Modified Plants (second ed.). Upon sporulation, B. thuringiensis forms proteinaceous insecticidal δ-endotoxins either in crystals (Cry toxins) or cytoplasmically (Cyt toxins), which are encoded by cry or cyt genes, respectively. When insects ingest toxin crystals, the enzymes in their digestive tract cause the toxin to become activated. The toxin binds to the insect's gut membranes, forming a pore that results in swelling, cell lysis, and eventually killing the insect. B. thuringiensis also produces insecticidal proteins at other stages in its lifecycle, specifically the vegetative insecticidal proteins (VIPs)
  3. ^
    PMID 7490762
    .
  4. ^ .
  5. .
  6. .
  7. ^ .
  8. ^ .
  9. ^ "Pesticidal crystal protein (IPR038979)". InterPro. Retrieved 12 April 2019.
  10. PMID 6443645
    .
  11. ^ "Species: Pesticidal crystal protein (IPR038979)". InterPro.
  12. ^ "Bacillus thuringiensis Toxin Nomenclature". Bt toxin specificity database. Retrieved 12 April 2019.
  13. PMID 10882663
    .
  14. .
  15. ^ "List of Parasporins". Committee of Parasporin Classification and Nomenclature. Accessed Jan 4, 2013
  16. ^ Crickmore N. "Other Cry Sequences" (PDF). Retrieved 12 April 2019.
  17. PMID 9729610
    .
  18. .
  19. ^ .
  20. .

Further reading

External links

This article incorporates text from the public domain Pfam and InterPro: IPR015790