Delta endotoxins

Delta endotoxin, N-terminal domain
crystal structure of the insecticidal bacterial del endotoxin Cry3Bb1 Bacillus thuringiensis[1]
Identifiers
SymbolEndotoxin_N
PfamPF03945
InterProIPR005639
SCOP21dlc / SCOPe / SUPFAM
TCDB1.C.2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Delta endotoxin, middle domain
Identifiers
SymbolEndotoxin_M
PfamPF00555
Pfam clanCL0568
InterProIPR015790
SCOP21dlc / SCOPe / SUPFAM
TCDB1.C.2
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Delta endotoxin, C-terminal
Identifiers
SymbolEndotoxin_C
PfamPF03944
Pfam clanCL0202
InterProIPR005638
SCOP21dlc / SCOPe / SUPFAM
TCDB1.C.2
CDDcd04085
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cytolytic delta-endotoxin Cyt1/2
Identifiers
SymbolCytB
PfamPF01338
InterProIPR001615
SCOP21cby / SCOPe / SUPFAM
TCDB1.C.71
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Delta endotoxins (δ-endotoxins) are a family of pore-forming toxins produced by Bacillus thuringiensis species of bacteria. They are useful for their insecticidal action and are the primary toxin produced by the genetically modified (GM) 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]

  1. ^ Galitsky N, Cody V, Wojtczak A, Ghosh D, Luft JR, Pangborn W, English L (August 2001). "Structure of the insecticidal bacterial delta-endotoxin Cry3Bb1 of Bacillus thuringiensis". Acta Crystallographica. Section D, Biological Crystallography. 57 (Pt 8): 1101–1109. doi:10.1107/S0907444901008186. 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)