Molecular characterization and functional expression of voltage‐gated sodium channel variants in <i>Apolygus lucorum</i> (<scp>Meyer‐Dür</scp>)

Pest Management Science

Duan

Gao

et al. 2021

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BACKGROUND Myzus persicae (Sulzer), a worldwide pest, has caused remarkable damage to agriculture. Among the various control methods, chemical control (especially pyrethroids) is most commonly used. The targets of pyrethroids are voltage‐gated sodium channels (Navs). Unlike those of other insects, all Navs of aphids (including two genes), such as Myzus persicae, are unique. RESULTS In this study, three interlock patterns, I(918)‐F(1014), L(918)‐L(1014), and T(918)‐F(1014), were found at sites 918 and 1014 in the sensitive Myzus persicae strain. Similar to that of other aphids, the Nav of Myzus persicae (MpNav) consisted of two parts, that is MpNav‐I and MpNav‐II, which were embedded with an atypical ‘DENS’ ion selectivity filter and a conventional ‘MFM’ inactivation gate, respectively. MpNav had 11 alternative exons, including two mutually exclusive exons (k and l) and three exons (w, x, and t), which were located in domains I and III, respectively. In addition, various RNA editing events, A503T and V588A, appearing between the connection of domains I and II and the S3 of domain IV, respectively, had been described. CONCLUSION Overall, MpNav was characterized by unique post‐translational regulation mode, 918 and 1014 interlocks, and unusually alternative exons. Our research provides a new perspective on the evolution and variation of insect Navs. © 2021 Society of Chemical Industry

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Unique post‐translational modifications diversify the sodium channels in peach aphid (Myzus persicae [Sulzer])

Pest Management Science

Duan

Gao

et al. 2021

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“…18 Our group successfully cloned and expressed AlNa v in Xenopus oocytes. 23 In this study, we found double mutations L 1002 F and M 906 I (L 2i16 F and M 2k11 I) which are in the domain II from field population of A.lucorum in China (L 1002 F in our research is the same amino acid position as L 1015 F in Zhen's research, for different variants). Although the double mutation was conferred to pyrethoids resistant in other insect species, we still need directly to prove the function of L 1002 F/ M 906 I in A. lucorum.…”

Section: Introductionmentioning

confidence: 47%

“…Zhen reported a population collected from Shandong Province that exhibited 30‐fold resistance to λ‐cyhalothrin, and mutation L 1015 F was detected only in the Shandong population in the AlNa v (sodium channel in A. lucorum ) 18 . Our group successfully cloned and expressed AlNa v in Xenopus oocytes 23 . In this study, we found double mutations L 1002 F and M 906 I (L 2i16 F and M 2k11 I) which are in the domain II from field population of A.lucorum in China (L 1002 F in our research is the same amino acid position as L 1015 F in Zhen’s research, for different variants).…”

Section: Introductionmentioning

confidence: 99%

Two classic mutations in the linker‐helix IIL45 and segment IIS6 of Apolygus lucorum sodium channel confer pyrethroid resistance

Lin

Pest Management Science

et al. 2020

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BACKGROUND: Pyrethroids are classified as type I and type II for distinct symptomology. Voltage-gated sodium channel is a primary target of pyrethroids. Mutations of the insect sodium channel have been identified to result in resistance to pyrethroids. Double mutation (L 1002 F/M 906 I) was detected in field-strain of Apolygus lucorum (Meyer-Dür). Although, it was illuminated the function of the same position mutation in other pests, it is necessary to demonstrate the role in A. lucorum. RESULTS: In this study, we examined the effects of mutations on channel gating and pyrethroid sensitivity in Xenopus oocytes. L 1002 F, M 906 I and L 1002 F/M 906 I all shifted the voltage dependence of activation in the depolarizing direction. L 1002 F, M 906 I and L 1002 F/M 906 I all reduced the amplitude of tail currents induced by type I (bifenthrin and permethrin) and type II (⊗-cyhalothrin and deltamethrin). The double mutation, L 1002 F/M 906 I, reduced integral channel modification by 10-fold compared with the L 1002 F and M 906 I mutations alone, respectively. Computational analysis based on the model of dual pyrethroid receptors, the two resistance mutations, L 1002 F and M 906 I are facing two opposite sides of this newly identified pocket. Both mutations affect the optimal binding of the ligands by changing the shape of the pocket but in different ways. CONCLUSION: Our results illustrate the distinct effect of mutations on pyrethroids. It is predicted with computer modeling that these mutations allosterically affect pyrethroid binding.

“…We adhered scrupulously to the rules for animal welfare and protection set forth by China, Hainan University, and international norms. Oocyte preparation, cRNA production, and injection techniques were the same as previously described . cRNA was created utilizing the mMESSAGE mMACHINE high-yield capped RNA kit and in vitro transcription with T7 polymerase (Ambion, Austin, TX, USA).…”

Section: Methodsmentioning

confidence: 99%

Functional Characterization of Knockdown Resistance Mutation L1014S in the German Cockroach, Blattella germanica (Linnaeus)

Liu

Zhang

et al. 2023

J. Agric. Food Chem.

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The effectiveness of pyrethroid insecticides is seriously threatened by knockdown resistance (kdr), which is induced in insects by inherited single-nucleotide polymorphisms in the voltage-gated sodium channel (VGSC) gene. VGSC's L1014F substitution results in the classic kdr mutation, which is found in many pest species. Other substitutions of the L1014 locus, such as L1014S, L1014C, L1014W, and L1014H, were also reported. In 2022, a new amino acid substitute L1014S of Blattella germanica was first discovered in China. We modified the BgNa v 1-1 sodium channel from cockroaches with the L1014S mutation to study how pyrethroid sensitivity and channel gating were affected in Xenopus oocytes. The L1014S mutation reduced the half-maximal activation voltage (V 1/2,act ) from −19.0 (wild type) to −15.5 mV while maintaining the voltage dependency of activation. Moreover, the voltage dependence of inactivation in the hyperpolarizing shifts from −48.3 (wild type) to −50.9 mV. However, compared with wild type, the mutation L1014S did not cause a significant shift in the half activation voltage (V 1/2,act ). Notably, the voltage dependency of activation was unaffected greatly by the L1014S mutation. Tail currents are induced by two types of pyrethroids (1 μM): type I (permethrin, bifenthrin) and type II (deltamethrin, λ-cyhalothrin). All four pyrethroids produced tail currents, and significant differences were found in the percentages of channel modifications between variants and wild types. Further computer modeling showed that the L1014S mutation allosterically modifies pyrethroid binding and action on B. germanica VGSC, with some residues playing a critical role in pyrethroid binding. This study elucidated the pyrethroid resistance mechanism of B. germanica and predicted the residues that may confer the risk of pyrethroid resistance, providing a molecular basis for understanding the resistance mechanisms conferred by mutations at the 1014 site in VGSC.