An insecticidal crystal protein (ICP) gene was cloned from Bacillus th
uringiensis strain AF101 which has a low toxicity to the silkworm, Bom
byx mori. The cloned AF101 ICP gene encoded 1,182 amino acid residues
and shared 93% homology with the cry1Ab gene of B. thuringiensis serov
ar kurstaki I-ID-I. In the amino-terminal portion of the activated tox
in region of AF101 ICP, there were 18 amino acid differences when comp
ared with HD-1 Cry1Ab, but only three amino acid differences in the hy
pervariable region of the activated toxin. The AF101 ICP gene was also
found to contain the Cys-rich region observed in cry1Aa and cry1Ac in
its carboxyl-terminal portion of the non-toxin region. In a bioassay
of the cloned gene product, toxicity with intact AF101 ICP was nearly
17% less than that of HD-1 Cry1Ab. On the other hand, the activated to
xin prepared from ICP by removing the non-toxin region was 9% less tha
n that of I-ID-I Cry1Ab. These results suggested that the specific tox
icity of AF101 ICP against the silkworm correlated not only with its a
ctivated toxin region, but also with the non-toxin region.