Correlation of the insecticidal activity of the Bacillus thuringiensis A4 strain against Bactrocera oleae (Diptera) with the 140-kDa crystal polypeptide.
The crystals of the soil-isolated Bacillus thuringiensis (Bt) strain A4 consist of two polypeptides with molecular mass of 140 kDa and 32 kDa that exhibit insecticidal activity against adult flies of Bactrocera oleae (Diptera). Plasmid curing applied to this strain resulted in the isolation of several subclones exhibiting alterations in their crystal polypeptides as well as two acrystalliferous subclones. The crystals of subclone 1.1 lacked the 32-kDa polypeptide and consisted uniquely of a 140-kDa polypeptide antigenically related to the parental 140-kDa crystal polypeptide. Additionally, the crystals of this subclone exhibited insecticidal activity against B. oleae equivalent to that of the parental strain. Therefore, the 32-kDa crystal polypeptide is dispensable for insecticidal activity, which appears to be dependent on the presence of the 140-kDa crystal polypeptide.
Sivropoulou
A
A
Laboratory of General Microbiology, Section of Genetics, Development and Molecular Biology, School of Biology, Aristotle University, Thessaloniki 54006, Greece. asivropo@bio.auth.gr
Haritidou
L
L
Vasara
E
E
Aptosoglou
S
S
Koliais
S
S
D000818:Animals; D001413:Bacillus thuringiensis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry / Q000494:pharmacology*; D001427:Bacterial Toxins / Q000737:chemistry / Q000494:pharmacology*; D003460:Crystallization; D004175:Diptera / Q000187:drug effects*; D007306:Insecticides / Q000494:pharmacology; D008970:Molecular Weight; D013170:Spores / Q000187:drug effects; D013997:Time Factors
D001426:Bacterial Proteins; D001427:Bacterial Toxins; D007306:Insecticides