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Comparative studies on acetylcholinesterase characteristics between the aphids, Sitobion avenae and Rhopalosiphum padi.

Lu YH, He YP, Gao XW - J. Insect Sci. (2013)

Bottom Line: The purification factor and yield from S. avenae (234.7-fold and 92.9%) were far higher than that from R. padi 17.3-fold and 13.9%.This suggests that eserine and BW284C51 may bind with other proteins, such as carboxylesterase, in the crude extract to reduce their inhibition against AChE.These results are useful for planning the chemical control of aphids on wheat.

View Article: PubMed Central - PubMed

Affiliation: Department of Entomology, China Agricultural University, Beijing 100193, China. luyanhui1211@gmail.com

ABSTRACT
The aphids Sitobion avenae (Fabricius) and Rhopalosiphum padi (Linnaeus) (Hemiptera: Aphidiae) are serious pests on grain crops and usually coexist on late period of wheat growth in China. Bioassays showed that R. padi was more susceptible than S. avenae to pirimicarb that is used for wheat aphid control, and the determination of acetylcholinesterase (AChE, EC 3.1.1.7) sensitivity showed that the sensitivity of AChE to pirimicarb was significantly higher in R. padi than in S. avenae ( Lu and Gao 2009 ). AChE is the target enzyme of the carbamates, including pirimicarb, hence, to understand the mechanism responsible for the tolerance difference to carbamate insecticides of S. avenae and R. padi, we purified AChE from both aphid species using procainamide affinity column and characterized the AChE. The purification factor and yield from S. avenae (234.7-fold and 92.9%) were far higher than that from R. padi 17.3-fold and 13.9%. The results of substrate and inhibitor specificities of purified enzyme from both S. avenae and R. padi indicated that the purified enzyme was a typical AChE. The crude AChE extract from S. avenae was 5.4-, 4.3- and 8.1-fold less sensitive to inhibition by pirimicarb, methomyl and thiodicarb, respectively, than that from R. padi, whereas for the purified AChE, S. avenae was only 1.6-, 1.3- and 1.7-fold less sensitive to inhibition by pirimicarb, methomyl and thiodicarb, respectively, than R. padi. This suggests that eserine and BW284C51 may bind with other proteins, such as carboxylesterase, in the crude extract to reduce their inhibition against AChE. These results are useful for planning the chemical control of aphids on wheat.

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Comparison of the elution profiles of AChE from the procainamide affinity column (1.0 × 5.5 cm) between Rhopalosiphum padi (a) and Sitobion avenae (b). Flow rate was 16 mL/h, and 1.0 mL fractions except fraction 1, which was 5.0 mL, were collected after the elution buffer containing 0.05 M tetraethylammonium iodide was applied. High quality figures are available online.
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f01_01: Comparison of the elution profiles of AChE from the procainamide affinity column (1.0 × 5.5 cm) between Rhopalosiphum padi (a) and Sitobion avenae (b). Flow rate was 16 mL/h, and 1.0 mL fractions except fraction 1, which was 5.0 mL, were collected after the elution buffer containing 0.05 M tetraethylammonium iodide was applied. High quality figures are available online.

Mentions: AChEs were purified from both S. avenae and R. padi by procanamide affinity chromatography. The shape of the elution curve for the AChE purification showed no obvious difference between S. avenae and R. padi (Figure 1). But the purification factor and yield were far higher for S. avenae than for R. padi. The overall purification factors and yields were 234.7-fold and 92.9 % for S. avenae, and 17.3-fold and 13.85 % for R. padi respectively (Table 1). The specific activity of AChE after purification by affinity column was 277.00 nmol/min/mg for S. avenae, significantly higher than in R. padi with the specific activity of AChE with 25.80 nmol/min/mg protein.


Comparative studies on acetylcholinesterase characteristics between the aphids, Sitobion avenae and Rhopalosiphum padi.

Lu YH, He YP, Gao XW - J. Insect Sci. (2013)

Comparison of the elution profiles of AChE from the procainamide affinity column (1.0 × 5.5 cm) between Rhopalosiphum padi (a) and Sitobion avenae (b). Flow rate was 16 mL/h, and 1.0 mL fractions except fraction 1, which was 5.0 mL, were collected after the elution buffer containing 0.05 M tetraethylammonium iodide was applied. High quality figures are available online.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3735166&req=5

f01_01: Comparison of the elution profiles of AChE from the procainamide affinity column (1.0 × 5.5 cm) between Rhopalosiphum padi (a) and Sitobion avenae (b). Flow rate was 16 mL/h, and 1.0 mL fractions except fraction 1, which was 5.0 mL, were collected after the elution buffer containing 0.05 M tetraethylammonium iodide was applied. High quality figures are available online.
Mentions: AChEs were purified from both S. avenae and R. padi by procanamide affinity chromatography. The shape of the elution curve for the AChE purification showed no obvious difference between S. avenae and R. padi (Figure 1). But the purification factor and yield were far higher for S. avenae than for R. padi. The overall purification factors and yields were 234.7-fold and 92.9 % for S. avenae, and 17.3-fold and 13.85 % for R. padi respectively (Table 1). The specific activity of AChE after purification by affinity column was 277.00 nmol/min/mg for S. avenae, significantly higher than in R. padi with the specific activity of AChE with 25.80 nmol/min/mg protein.

Bottom Line: The purification factor and yield from S. avenae (234.7-fold and 92.9%) were far higher than that from R. padi 17.3-fold and 13.9%.This suggests that eserine and BW284C51 may bind with other proteins, such as carboxylesterase, in the crude extract to reduce their inhibition against AChE.These results are useful for planning the chemical control of aphids on wheat.

View Article: PubMed Central - PubMed

Affiliation: Department of Entomology, China Agricultural University, Beijing 100193, China. luyanhui1211@gmail.com

ABSTRACT
The aphids Sitobion avenae (Fabricius) and Rhopalosiphum padi (Linnaeus) (Hemiptera: Aphidiae) are serious pests on grain crops and usually coexist on late period of wheat growth in China. Bioassays showed that R. padi was more susceptible than S. avenae to pirimicarb that is used for wheat aphid control, and the determination of acetylcholinesterase (AChE, EC 3.1.1.7) sensitivity showed that the sensitivity of AChE to pirimicarb was significantly higher in R. padi than in S. avenae ( Lu and Gao 2009 ). AChE is the target enzyme of the carbamates, including pirimicarb, hence, to understand the mechanism responsible for the tolerance difference to carbamate insecticides of S. avenae and R. padi, we purified AChE from both aphid species using procainamide affinity column and characterized the AChE. The purification factor and yield from S. avenae (234.7-fold and 92.9%) were far higher than that from R. padi 17.3-fold and 13.9%. The results of substrate and inhibitor specificities of purified enzyme from both S. avenae and R. padi indicated that the purified enzyme was a typical AChE. The crude AChE extract from S. avenae was 5.4-, 4.3- and 8.1-fold less sensitive to inhibition by pirimicarb, methomyl and thiodicarb, respectively, than that from R. padi, whereas for the purified AChE, S. avenae was only 1.6-, 1.3- and 1.7-fold less sensitive to inhibition by pirimicarb, methomyl and thiodicarb, respectively, than R. padi. This suggests that eserine and BW284C51 may bind with other proteins, such as carboxylesterase, in the crude extract to reduce their inhibition against AChE. These results are useful for planning the chemical control of aphids on wheat.

Show MeSH
Related in: MedlinePlus