Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin

Makoto Ihara; Toshihide Okajima; Atsuko Yamashita; Takuma Oda; Koichi Hirata; Hisashi Nishiwaki; Takako Morimoto; Miki Akamatsu; Yuji Ashikawa; Shun'Ichi Kuroda; Ryosuke Mega; Seiki Kuramitsu; David B. Sattelle; Kazuhiko Matsuda

doi:10.1007/s10158-008-0069-3

Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin

Makoto Ihara, Toshihide Okajima, Atsuko Yamashita, Takuma Oda, Koichi Hirata, Hisashi Nishiwaki, Takako Morimoto, Miki Akamatsu, Yuji Ashikawa, Shun'Ichi Kuroda, Ryosuke Mega, Seiki Kuramitsu, David B. Sattelle, Kazuhiko Matsuda

Research output: Contribution to journal › Article › peer-review

Abstract

Neonicotinoid insecticides, which act on nicotinic acetylcholine receptors (nAChRs) in a variety of ways, have extremely low mammalian toxicity, yet the molecular basis of such actions is poorly understood. To elucidate the molecular basis for nAChR-neonicotinoid interactions, a surrogate protein, acetylcholine binding protein from Lymnaea stagnalis (Ls-AChBP) was crystallized in complex with neonicotinoid insecticides imidacloprid (IMI) or clothianidin (CTD). The crystal structures suggested that the guanidine moiety of IMI and CTD stacks with Tyr185, while the nitro group of IMI but not of CTD makes a hydrogen bond with Gln55. IMI showed higher binding affinity for Ls-AChBP than that of CTD, consistent with weaker CH-π interactions in the Ls-AChBP-CTD complex than in the Ls-AChBP-IMI complex and the lack of the nitro group-Gln55 hydrogen bond in CTD. Yet, the NH at position 1 of CTD makes a hydrogen bond with the backbone carbonyl of Trp143, offering an explanation for the diverse actions of neonicotinoids on nAChRs. © 2008 The Author(s).

Original language	English
Pages (from-to)	71-81
Number of pages	10
Journal	Invertebrate Neuroscience
Volume	8
Issue number	2
DOIs	https://doi.org/10.1007/s10158-008-0069-3
Publication status	Published - Jun 2008

Keywords

Acetylcholine binding protein (Lymnaea stagnalis)
Crystal structures
Ion channels
Neonicotinoids
Nicotinic acetylcholine receptors

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10.1007/s10158-008-0069-3

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Ihara, M., Okajima, T., Yamashita, A., Oda, T., Hirata, K., Nishiwaki, H., Morimoto, T., Akamatsu, M., Ashikawa, Y., Kuroda, SI., Mega, R., Kuramitsu, S., Sattelle, D. B., & Matsuda, K. (2008). Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin. Invertebrate Neuroscience, 8(2), 71-81. https://doi.org/10.1007/s10158-008-0069-3

@article{1b311e55d7fd476ea05c2e4e4c3c5f15,

title = "Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin",

abstract = "Neonicotinoid insecticides, which act on nicotinic acetylcholine receptors (nAChRs) in a variety of ways, have extremely low mammalian toxicity, yet the molecular basis of such actions is poorly understood. To elucidate the molecular basis for nAChR-neonicotinoid interactions, a surrogate protein, acetylcholine binding protein from Lymnaea stagnalis (Ls-AChBP) was crystallized in complex with neonicotinoid insecticides imidacloprid (IMI) or clothianidin (CTD). The crystal structures suggested that the guanidine moiety of IMI and CTD stacks with Tyr185, while the nitro group of IMI but not of CTD makes a hydrogen bond with Gln55. IMI showed higher binding affinity for Ls-AChBP than that of CTD, consistent with weaker CH-π interactions in the Ls-AChBP-CTD complex than in the Ls-AChBP-IMI complex and the lack of the nitro group-Gln55 hydrogen bond in CTD. Yet, the NH at position 1 of CTD makes a hydrogen bond with the backbone carbonyl of Trp143, offering an explanation for the diverse actions of neonicotinoids on nAChRs. {\textcopyright} 2008 The Author(s).",

keywords = "Acetylcholine binding protein (Lymnaea stagnalis), Crystal structures, Ion channels, Neonicotinoids, Nicotinic acetylcholine receptors",

author = "Makoto Ihara and Toshihide Okajima and Atsuko Yamashita and Takuma Oda and Koichi Hirata and Hisashi Nishiwaki and Takako Morimoto and Miki Akamatsu and Yuji Ashikawa and Shun'Ichi Kuroda and Ryosuke Mega and Seiki Kuramitsu and Sattelle, {David B.} and Kazuhiko Matsuda",

note = ", Medical Research Council, United Kingdom",

year = "2008",

month = jun,

doi = "10.1007/s10158-008-0069-3",

language = "English",

volume = "8",

pages = "71--81",

journal = "Invertebrate Neuroscience",

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Ihara, M, Okajima, T, Yamashita, A, Oda, T, Hirata, K, Nishiwaki, H, Morimoto, T, Akamatsu, M, Ashikawa, Y, Kuroda, SI, Mega, R, Kuramitsu, S, Sattelle, DB & Matsuda, K 2008, 'Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin', Invertebrate Neuroscience, vol. 8, no. 2, pp. 71-81. https://doi.org/10.1007/s10158-008-0069-3

TY - JOUR

T1 - Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin

AU - Ihara, Makoto

AU - Okajima, Toshihide

AU - Yamashita, Atsuko

AU - Oda, Takuma

AU - Hirata, Koichi

AU - Nishiwaki, Hisashi

AU - Morimoto, Takako

AU - Akamatsu, Miki

AU - Ashikawa, Yuji

AU - Kuroda, Shun'Ichi

AU - Mega, Ryosuke

AU - Kuramitsu, Seiki

AU - Sattelle, David B.

AU - Matsuda, Kazuhiko

N1 - , Medical Research Council, United Kingdom

PY - 2008/6

Y1 - 2008/6

N2 - Neonicotinoid insecticides, which act on nicotinic acetylcholine receptors (nAChRs) in a variety of ways, have extremely low mammalian toxicity, yet the molecular basis of such actions is poorly understood. To elucidate the molecular basis for nAChR-neonicotinoid interactions, a surrogate protein, acetylcholine binding protein from Lymnaea stagnalis (Ls-AChBP) was crystallized in complex with neonicotinoid insecticides imidacloprid (IMI) or clothianidin (CTD). The crystal structures suggested that the guanidine moiety of IMI and CTD stacks with Tyr185, while the nitro group of IMI but not of CTD makes a hydrogen bond with Gln55. IMI showed higher binding affinity for Ls-AChBP than that of CTD, consistent with weaker CH-π interactions in the Ls-AChBP-CTD complex than in the Ls-AChBP-IMI complex and the lack of the nitro group-Gln55 hydrogen bond in CTD. Yet, the NH at position 1 of CTD makes a hydrogen bond with the backbone carbonyl of Trp143, offering an explanation for the diverse actions of neonicotinoids on nAChRs. © 2008 The Author(s).

AB - Neonicotinoid insecticides, which act on nicotinic acetylcholine receptors (nAChRs) in a variety of ways, have extremely low mammalian toxicity, yet the molecular basis of such actions is poorly understood. To elucidate the molecular basis for nAChR-neonicotinoid interactions, a surrogate protein, acetylcholine binding protein from Lymnaea stagnalis (Ls-AChBP) was crystallized in complex with neonicotinoid insecticides imidacloprid (IMI) or clothianidin (CTD). The crystal structures suggested that the guanidine moiety of IMI and CTD stacks with Tyr185, while the nitro group of IMI but not of CTD makes a hydrogen bond with Gln55. IMI showed higher binding affinity for Ls-AChBP than that of CTD, consistent with weaker CH-π interactions in the Ls-AChBP-CTD complex than in the Ls-AChBP-IMI complex and the lack of the nitro group-Gln55 hydrogen bond in CTD. Yet, the NH at position 1 of CTD makes a hydrogen bond with the backbone carbonyl of Trp143, offering an explanation for the diverse actions of neonicotinoids on nAChRs. © 2008 The Author(s).

KW - Acetylcholine binding protein (Lymnaea stagnalis)

KW - Crystal structures

KW - Ion channels

KW - Neonicotinoids

KW - Nicotinic acetylcholine receptors

U2 - 10.1007/s10158-008-0069-3

DO - 10.1007/s10158-008-0069-3

M3 - Article

C2 - 18338186

SN - 1354-2516

VL - 8

SP - 71

EP - 81

JO - Invertebrate Neuroscience

JF - Invertebrate Neuroscience

IS - 2

ER -

Crystal structures of Lymnaea stagnalis AChBP in complex with neonicotinoid insecticides imidacloprid and clothianidin

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Keywords

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