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Chimeric Investigations into the Diamide Binding Site on the Lepidopteran Ryanodine Receptor

Ewan Richardson, Bartek J. Troczka, Oliver Gutbrod, Ulrich Ebbinghaus-Kintscher, Martin S. Williamson, Christopher George Orcid Logo, Ralf Nauen, Thomas G. Emyr Davies

International Journal of Molecular Sciences, Volume: 22, Issue: 23, Start page: 13033

Swansea University Author: Christopher George Orcid Logo

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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...

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Published in: International Journal of Molecular Sciences
ISSN: 1422-0067
Published: MDPI AG 2021
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URI: https://cronfa.swan.ac.uk/Record/cronfa58894
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spelling 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
container_volume 22
container_issue 23
container_start_page 13033
publishDate 2021
institution Swansea University
issn 1422-0067
doi_str_mv 10.3390/ijms222313033
publisher MDPI AG
college_str Faculty of Medicine, Health and Life Sciences
hierarchytype
hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine
document_store_str 1
active_str 0
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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score 11.017731

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