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Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor
International Journal of Molecular Sciences, Volume: 22, Issue: 23, Start page: 13033
Swansea University Author: Christopher George
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DOI (Published version): 10.3390/ijms222313033
Abstract
Alterations to amino acid residues G4946 and I4790, associated with resistance to diamide insecticides, suggests a location of diamide interaction within the pVSD voltage sensor-like domain of the insect ryanodine receptor (RyR). To further delineate the interaction site(s), targeted alterations wer...
Published in: | International Journal of Molecular Sciences |
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ISSN: | 1422-0067 |
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2021
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URI: | https://cronfa.swan.ac.uk/Record/cronfa58894 |
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2021-12-31T12:40:35.0862052 v2 58894 2021-12-06 Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor a2e211f7bd379c81e9c393637803a0a0 0000-0001-9852-1135 Christopher George Christopher George true false 2021-12-06 BMS Alterations to amino acid residues G4946 and I4790, associated with resistance to diamide insecticides, suggests a location of diamide interaction within the pVSD voltage sensor-like domain of the insect ryanodine receptor (RyR). To further delineate the interaction site(s), targeted alterations were made within the same pVSD region on the diamondback moth (Plutella xylostella) RyR channel. The editing of five amino acid positions to match those found in the diamide insensitive skeletal RyR1 of humans (hRyR1) in order to generate a human−Plutella chimeric construct showed that these alterations strongly reduce diamide efficacy when introduced in combination but cause only minor reductions when introduced individually. It is concluded that the sites of diamide interaction on insect RyRs lie proximal to the voltage sensor-like domain of the RyR and that the main site of interaction is at residues K4700, Y4701, I4790 and S4919 in the S1 to S4 transmembrane domains. Journal Article International Journal of Molecular Sciences 22 23 13033 MDPI AG 1422-0067 diamide insecticides, chlorantraniliprole, flubendiamide, lepidoptera, Plutella xylostella, binding site 2 12 2021 2021-12-02 10.3390/ijms222313033 COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University Another institution paid the OA fee Bayer CropScience through a Biotechnology and Biological Sciences Research Council-funded Industrial studentship (BBSRC grant NoBB/N504075/1); Biotechnology and Biological Sciences Research Council, UK. 2021-12-31T12:40:35.0862052 2021-12-06T10:47:52.3802154 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Ewan Richardson 1 Bartek J. Troczka 2 Oliver Gutbrod 3 Ulrich Ebbinghaus-Kintscher 4 Martin S. Williamson 5 Christopher George 0000-0001-9852-1135 6 Ralf Nauen 7 Thomas G. Emyr Davies 8 58894__21796__a3773f2c20dd47818ffefdf72b9519c4.pdf ijms-22-13033.pdf 2021-12-06T10:47:52.3801697 Output 2377370 application/pdf Version of Record true © 2021 by the authors.This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license true eng https://creativecommons.org/licenses/by/4.0/ |
title |
Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor |
spellingShingle |
Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor Christopher George |
title_short |
Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor |
title_full |
Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor |
title_fullStr |
Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor |
title_full_unstemmed |
Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor |
title_sort |
Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor |
author_id_str_mv |
a2e211f7bd379c81e9c393637803a0a0 |
author_id_fullname_str_mv |
a2e211f7bd379c81e9c393637803a0a0_***_Christopher George |
author |
Christopher George |
author2 |
Ewan Richardson Bartek J. Troczka Oliver Gutbrod Ulrich Ebbinghaus-Kintscher Martin S. Williamson Christopher George Ralf Nauen Thomas G. Emyr Davies |
format |
Journal article |
container_title |
International Journal of Molecular Sciences |
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22 |
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23 |
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13033 |
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2021 |
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Swansea University |
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1422-0067 |
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10.3390/ijms222313033 |
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MDPI AG |
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Faculty of Medicine, Health and Life Sciences |
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Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine |
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description |
Alterations to amino acid residues G4946 and I4790, associated with resistance to diamide insecticides, suggests a location of diamide interaction within the pVSD voltage sensor-like domain of the insect ryanodine receptor (RyR). To further delineate the interaction site(s), targeted alterations were made within the same pVSD region on the diamondback moth (Plutella xylostella) RyR channel. The editing of five amino acid positions to match those found in the diamide insensitive skeletal RyR1 of humans (hRyR1) in order to generate a human−Plutella chimeric construct showed that these alterations strongly reduce diamide efficacy when introduced in combination but cause only minor reductions when introduced individually. It is concluded that the sites of diamide interaction on insect RyRs lie proximal to the voltage sensor-like domain of the RyR and that the main site of interaction is at residues K4700, Y4701, I4790 and S4919 in the S1 to S4 transmembrane domains. |
published_date |
2021-12-02T04:15:47Z |
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1763754059861327872 |
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11.028886 |