Similarity in moth-fly specific larvicidal activity between two serologically unrelated Bacillus thuringiensis strains.
Parasporal inclusions of a Bacillus thuringiensis isolate designated 92-KU-105-9 (H14/19) exhibited unusual larvicidal activity, specific for the moth-fly, Telmatoscopus albipunctatus (Diptera: Psychodidae), similar to that of a previously reported B. thuringiensis serovar leesis (H33) strain. The LC50 value of the purified inclusions was 4.92 micrograms ml-1 for the moth-fly larvae, while no mortality was shown in the mosquitoes Culex pipiens molestus and Anopheles stephensi, at protein concentrations up to 10 mg ml-1. Morphologically, the inclusion was a homogeneous globular body surrounded by an electron-dense, thick envelope. Multilamellar inner structure was evident between envelope membrane and inclusion matrix. SDS-PAGE revealed that the inclusions consist of five proteins with molecular masses of 72, 70, 68, 56 and 30 kDa. These proteins cross-reacted with the antibodies against inclusion proteins of the serovar leesis strain. High homologies existed in N-terminal amino acid sequences between the three major proteins (72, 70 and 68 kDa) and the two established protein classes, Cry4A and Cry10A.
Higuchi
K
K
Section of Applied Microbiology, Fukuoka Industrial Technology Center, Japan.
Saitoh
H
H
Mizuki
E
E
Ohba
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001413:Bacillus thuringiensis / Q000737:chemistry / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000737:chemistry / Q000276:immunology*; D006801:Humans; D002479:Inclusion Bodies / Q000737:chemistry* / Q000235:genetics; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D009036:Moths; D010572:Pest Control, Biological / Q000379:methods*; D011576:Psychodidae; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D001426:Bacterial Proteins