Differential Activity and Activation of Bacillus thuringiensis Insecticidal Proteins in Diamondback Moth, Plutella xylostella

1999 ◽  
Vol 39 (3) ◽  
pp. 159-162 ◽  
Author(s):  
Rose Monnerat *, § , Luke Masson ◽  
Roland Brousseau ◽  
Marianne Pusztai-Carey ◽  
Dominique Bordat ◽  
Roger Frutos
Keyword(s):  
Bacillus Thuringiensis ◽  
Plutella Xylostella ◽  
Diamondback Moth ◽  
Insecticidal Proteins

Enhancement of δ-Endotoxin Activity by Toxin-Free Spore of Bacillus thuringiensis against the Diamondback Moth, Plutella xylostella

1994 ◽  
Vol 63 (1) ◽  
pp. 111-112 ◽  
Author(s):  
Minoru Miyasono ◽  
Shyuichiro Inagaki ◽  
Makiko Yamamoto ◽  
Katsuaki Ohba ◽  
Takeo Ishiguro ◽  
...  
Keyword(s):  
Bacillus Thuringiensis ◽  
Plutella Xylostella ◽  
Diamondback Moth ◽  
Endotoxin Activity ◽  
Free Spore

scholarly journals Insecticidal Effects of Organotin(IV) Compounds on Plutella Xylostella (L.) Larvae. II. Inhibitory Potencies Against Acetylcholinesterase and Evidence for Synergism in Tests With Bacillus Thuringiensis(BER.) and Malathion

1994 ◽  
Vol 1 (1) ◽  
pp. 1-17 ◽  
Author(s):  
Nazni W. Ahmad ◽  
Tay Siew Huang ◽  
S. Balabaskaran ◽  
K. M. Lo ◽  
V. G. Kumar Das
Keyword(s):  
Bacillus Thuringiensis ◽  
Plutella Xylostella ◽  
Resistant Strain ◽  
Synergistic Effects ◽  
Diamondback Moth ◽  
Ache Inhibition ◽  
Microbial Insecticide ◽  
In Vitro Inhibition ◽  
Sublethal Concentrations

Features of pesticide synergism and acetylcholinesterase (AChE) inhibition (in vitro) were studied using a selected range of organotin compounds against the early 4th instar larvae of a highly resistant strain of the diamondback moth (DBM), Plutella xylostella, a major universal pest of cruciferous vegetables.Fourteen triorganotin compounds were evaluated for their ability to enhance the toxicity of the microbial insecticide, Bacillus thuringiensis (BT) and of the commercial insecticide, Malathion to Plutella xylostella larvae. Supplemental synergism was observed with triphenyl- and tricyclopentyltin hydroxides in combinations with Bacillus thuringiensis. Increased synergism was observed with an increase in the number of cyclopentyl groups on tin in the mixed series, CypnPh3-n SnX, where X = OH, and 1-(1,2,4-triazolyl). The combination of (p-chlorophenyl)diphenyltin N,N-dimethyldithiocarbamate at LD10 and LD25 concentrations with sublethal concentrations of Malathion as well as of tricyclohexyltin methanesulphonate at the 0.01% (w/v) concentration with Malathion exerted strong synergistic effects (supplemental synergism) with toxicity index (T.I) values of 7.2, 19.8 and 10.1, respectively.Studies on the in vitro inhibition of acetylcholinesterase prepared from the DBM larvae showed that while most of the triorganotin Compounds tested were without effect on the enzyme, compounds containing the thiocarbamylacetate or the dithiocarbamylacetate moieties demonstrated appreciable levels of inhibition, being comparable in efficacy to commercial grades of Malathion and Methomyl.

Integrative Model for Binding of Bacillus thuringiensis Toxins in Susceptible and Resistant Larvae of the Diamondback Moth (Plutella xylostella)

1999 ◽  
Vol 65 (4) ◽  
pp. 1413-1419 ◽  
Author(s):  
Victoria Ballester ◽  
Francisco Granero ◽  
Bruce E. Tabashnik ◽  
Thomas Malvar ◽  
Juan Ferré
Keyword(s):  
Bacillus Thuringiensis ◽  
Plutella Xylostella ◽  
Binding Sites ◽  
Diamondback Moth ◽  
The Philippines ◽  
Competitive Binding ◽  
Single Mutation ◽  
Crystal Proteins ◽  
Mechanism Of Resistance ◽  
Resistant Strains

ABSTRACT Insecticidal crystal proteins from Bacillus thuringiensis in sprays and transgenic crops are extremely useful for environmentally sound pest management, but their long-term efficacy is threatened by evolution of resistance by target pests. The diamondback moth (Plutella xylostella) is the first insect to evolve resistance to B. thuringiensis in open-field populations. The only known mechanism of resistance to B. thuringiensis in the diamondback moth is reduced binding of toxin to midgut binding sites. In the present work we analyzed competitive binding of B. thuringiensis toxins Cry1Aa, Cry1Ab, Cry1Ac, and Cry1F to brush border membrane vesicles from larval midguts in a susceptible strain and in resistant strains from the Philippines, Hawaii, and Pennsylvania. Based on the results, we propose a model for binding of B. thuringiensis crystal proteins in susceptible larvae with two binding sites for Cry1Aa, one of which is shared with Cry1Ab, Cry1Ac, and Cry1F. Our results show that the common binding site is altered in each of the three resistant strains. In the strain from the Philippines, the alteration reduced binding of Cry1Ab but did not affect binding of the other crystal proteins. In the resistant strains from Hawaii and Pennsylvania, the alteration affected binding of Cry1Aa, Cry1Ab, Cry1Ac, and Cry1F. Previously reported evidence that a single mutation can confer resistance to Cry1Ab, Cry1Ac, and Cry1F corresponds to expectations based on the binding model. However, the following two other observations do not: the mutation in the Philippines strain affected binding of only Cry1Ab, and one mutation was sufficient for resistance to Cry1Aa. The imperfect correspondence between the model and observations suggests that reduced binding is not the only mechanism of resistance in the diamondback moth and that some, but not all, patterns of resistance and cross-resistance can be predicted correctly from the results of competitive binding analyses of susceptible strains.

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