Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi

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 co...

Full description

Bibliographic Details
Main Authors:	Lu, Y. H., He, Y. P., Gao, X. W.
Format:	Online
Language:	English
Published:	University of Wisconsin Library 2013
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3735166/

id	pubmed-3735166
recordtype	oai_dc
spelling	pubmed-37351662013-08-08 Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi Lu, Y. H. He, Y. P. Gao, X. W. Article 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. University of Wisconsin Library 2013-01-31 /pmc/articles/PMC3735166/ /pubmed/23879406 http://dx.doi.org/10.1673/031.013.0901 Text en © 2013 http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Lu, Y. H. He, Y. P. Gao, X. W.
spellingShingle	Lu, Y. H. He, Y. P. Gao, X. W. Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi
author_facet	Lu, Y. H. He, Y. P. Gao, X. W.
author_sort	Lu, Y. H.
title	Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi
title_short	Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi
title_full	Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi
title_fullStr	Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi
title_full_unstemmed	Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi
title_sort	comparative studies on acetylcholinesterase characteristics between the aphids, sitobion avenae and rhopalosiphum padi
description	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.
publisher	University of Wisconsin Library
publishDate	2013
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3735166/
_version_	1612001090693234688

Comparative Studies on Acetylcholinesterase Characteristics between the Aphids, Sitobion avenae and Rhopalosiphum padi

Similar Items