400 resultados para Gypsy moth


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The Gypsy moth is a serious pest of trees ans shrubs. It damages the plants when the caterpillar stage eats the leaves. When there are many caterpillars, They defoliate entire trees, which can weaken and sometimes kill the trees. The gypsy moth is a notorious hitchhiker; it has been brought into Iowa on recreations vehicles and nursery stock. Learning the recognize the gypsy moth is an important part of preventing infestations and severe damage to Iowa's forests, woodlands, and urban landscapes.

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Substitutions or deletions of domain II loop residues of Bacillus thuringiensis δ-endotoxin CryIAb were constructed using site-directed mutagenesis techniques to investigate their functional roles in receptor binding and toxicity toward gypsy moth (Lymantria dispar). Substitution of loop 2 residue N372 with Ala or Gly (N372A, N372G) increased the toxicity against gypsy moth larvae 8-fold and enhanced binding affinity to gypsy moth midgut brush border membrane vesicles (BBMV) ≈4-fold. Deletion of N372 (D3), however, substantially reduced toxicity (>21 times) as well as binding affinity, suggesting that residue N372 is involved in receptor binding. Interestingly, a triple mutant, DF-1 (N372A, A282G and L283S), has a 36-fold increase in toxicity to gypsy moth neonates compared with wild-type toxin. The enhanced activity of DF-1 was correlated with higher binding affinity (18-fold) and binding site concentrations. Dissociation binding assays suggested that the off-rate of the BBMV-bound mutant toxins was similar to that of the wild type. However, DF-1 toxin bound 4 times more than the wild-type and N372A toxins, and it was directly correlated with binding affinity and potency. Protein blots of gypsy moth BBMV probed with labeled N372A, DF-1, and CryIAb toxins recognized a common 210-kDa protein, indicating that the increased activity of the mutants was not caused by binding to additional receptor(s). The improved binding affinity of N372A and DF-1 suggest that a shorter side chain at these loops may fit the toxin more efficiently to the binding pockets. These results offer an excellent model system for engineering δ-endotoxins with higher potency and wider spectra of target pests by improving receptor binding interactions.

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Cover title.

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Mode of access: Internet.

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At head of title: Environmental assessment.

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Contains also: Senate doc. no. 6 and Reports dated 1897, 1898 and Jan. 1907.

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"Issued August 1983"--P. [12]

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Shipping list no.: 91-0394-P.

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"October 1982"--P. [1].

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Shipping list no.: 94-0114-P.