The delta-endotoxin protein family displays a hydrophobic motif that might be implicated in toxicity.
A computer-based analysis of hydropathy and surface probability of representative members of each class of the Cry family of proteins was performed. A highly conserved hydrophobic motif within the previously described block, D2, is present not only in lepidopteran toxin genes but also in toxins active against diptera and coleoptera. An interesting feature of this hydrophobic motif is the presence of an aspartic residue (highly hydrophilic) in its middle part. Comparison with the amino acid sequence from diphtheria toxin showed that it also contains a hydrophobic motif similar to the one present in the Bacillus thuringiensis toxins. It also contains an aspartic residue in the middle part and some speculations are presented on the function of this specific region with regard to the toxic mechanism of action.
Pereyra-Alférez
B
B
Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos.
Bravo
A
A
Quintero
R
R
Soberón
X
X
D000595:Amino Acid Sequence; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins / Q000737:chemistry* / Q000145:classification / Q000633:toxicity*; D006460:Hemolysin Proteins; D008969:Molecular Sequence Data; D010572:Pest Control, Biological; D011487:Protein Conformation; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D013499:Surface Properties
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis