Insecticide Resistance of the Small Brown Planthopper, Laodelphax striatellus FALLEN (Hemiptera : Delphacidae), Collected in Kyushu and on the East China Sea

Nagata, Toru; Ohira, Yoshio

doi:10.1303/aez.21.216

Cited by 7 publications

(2 citation statements)

References 4 publications

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“…In a wide range of species, the elevation of esterase activity is the major mechanism of organophosphorus insecticide (OP) resistance [1][2][3][4][5][6][7][8]. The molecular basis of this resistance mechanism has only been extensively studied in two species.…”

Section: Introductionmentioning

confidence: 99%

Co-amplification explains linkage disequilibrium of two mosquito esterase genes in insecticide-resistant Culex quinquefasciatus

Vaughan

Hawkes

Hemingway

1997

Biochemical Journal

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The mosquito Culexquinquefasciatus (Say) is a vector of human disease and a world-wide biting nuisance. Organophosphorus insecticides (OPs) have been widely used to control C. quinquefasciatus populations and this has led to the emergence of OP-resistance. Predominantly, resistance is caused by increased production of two non-specific carboxylesterases, Estα21 and Estβ21. Increased abundance of these esterases is associated with the amplification of their respective genes. The estα21 and estβ21 genes were cloned and sequenced from OP-resistant Sri Lankan C. quinquefasciatus; the two adjacent genes are in a head to head configuration, within a single amplification unit (amplicon). The homology between the two genes suggests that they arose from an ancient duplication event. The two genes have different numbers of exons (estα21 has seven and estβ21 has four); however, the intron/exon boundaries in estβ21 are all conserved in estα21. The two genes are co-amplified in three other mosquito strains with the elevated Estα21/Estβ21 phenotype. Their complete linkage disequilibrium is explained by the location of the two genes involved in resistance within a single amplicon. In insecticide-susceptible C. quinquefasciatus, the non-amplified estα and estβ gene loci are also found in a similar head to head configuration, but the size of the intergenic non-coding region is approx. 1 kb less than in the amplicon. The smaller intergenic spacer is also found in a strain with amplified estβ11, which suggests that extensive laboratory selection for this amplified esterase has not eliminated the non-amplified genes. The intergenic spacer regions have been subcloned and sequenced. They contain numerous possible TATA boxes, promoters and a number of possible regulatory elements with high homology to the consensus sequence of the Barbie box. These latter putative regulatory elements are more numerous in the larger intergenic spacer, which differs from the non-amplified spacer by two large (> 420 bp) and one small (5 bp) insertions.

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Section: Introductionmentioning

confidence: 99%

Co-amplification explains linkage disequilibrium of two mosquito esterase genes in insecticide-resistant Culex quinquefasciatus

Vaughan

Hawkes

Hemingway

1997

Biochemical Journal

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“…The small brown planthopper Laodelphax striatellus is an important pest of rice, maize, and wheat. Insects can be controlled using chemical insecticides; however, the long-term use of chemical control leads to the development of a serious resistance to insecticides, such as organophosphates and carbamates [ 3 , 4 ], neonicotinoids, pyrethroids, and insect growth regulators [ 5 , 6 ]. In China, imidacloprid, along with buprofezin and certain other insecticides, was recommended for controlling planthoppers when these insects developed resistance to chlorpyrifos.…”

Section: Introductionmentioning

confidence: 99%

Buprofezin Is Metabolized by CYP353D1v2, a Cytochrome P450 Associated with Imidacloprid Resistance in Laodelphax striatellus

Elzaki

Miah

Han

2017

IJMS

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CYP353D1v2 is a cytochrome P450 related to imidacloprid resistance in Laodelphax striatellus. This work was conducted to examine the ability of CYP353D1v2 to metabolize other insecticides. Carbon monoxide difference spectra analysis indicates that CYP353D1v2 was successfully expressed in insect cell Sf9. The catalytic activity of CYP353D1v2 relating to degrading buprofezin, chlorpyrifos, and deltamethrin was tested by measuring substrate depletion and analyzing the formation of metabolites. The results showed the nicotinamide–adenine dinucleotide phosphate (NADPH)-dependent depletion of buprofezin (eluting at 8.7 min) and parallel formation of an unknown metabolite (eluting 9.5 min). However, CYP353D1v2 is unable to metabolize deltamethrin and chlorpyrifos. The recombinant CYP353D1v2 protein efficiently catalyzed the model substrate p-nitroanisole with a maximum velocity of 9.24 nmol/min/mg of protein and a Michaelis constant of Km = 6.21 µM. In addition, imidacloprid was metabolized in vitro by the recombinant CYP353D1v2 microsomes (catalytic constant Kcat) 0.064 pmol/min/pmol P450, Km = 6.41 µM. The mass spectrum of UPLC-MS analysis shows that the metabolite was a product of buprofezin, which was buprofezin sulfone. This result provided direct evidence that L. striatellus cytochrome P450 CYP353D1v2 is capable of metabolizing imidacloprid and buprofezin.

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Laodelphax striatellus (small brown planthopper)

2022

CABI Compendium

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Insecticide Resistance of the Small Brown Planthopper, Laodelphax striatellus FALLEN (Hemiptera : Delphacidae), Collected in Kyushu and on the East China Sea

Cited by 7 publications

References 4 publications

Co-amplification explains linkage disequilibrium of two mosquito esterase genes in insecticide-resistant Culex quinquefasciatus

Co-amplification explains linkage disequilibrium of two mosquito esterase genes in insecticide-resistant Culex quinquefasciatus

Buprofezin Is Metabolized by CYP353D1v2, a Cytochrome P450 Associated with Imidacloprid Resistance in Laodelphax striatellus

Laodelphax striatellus (small brown planthopper)

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