Charge substitutions at the voltage-sensing module of domain III enhance actions of site-3 and site-4 toxins on an insect sodium channel
文献类型： 外文期刊
作者： Zhu, Qing 1 ; Du, Yuzhe 2 ; Nomura, Yoshiko 2 ; Gao, Rong 3 ; Cang, Zixuan 4 ; Wei, Guo-Wei 4 ; Gordon, Dalia 5 ; Gurevit 1 ;
作者机构： 1.Jiangsu Acad Agr Sci, Key Lab Control Technol & Stand Agroprod Safety &, Key Lab Food Qual & Safety Jiangsu Prov, Minist Agr,Inst Food Safety & Nutr,State Key Lab, Nanjing, Peoples R China
2.Michigan State Univ, Dept Entomol, E Lansing, MI 48824 USA
3.Nanjing Med Univ, Dept Hyg Anal & Detect, Sch Publ Hlth, 818 Tianyuan East Rd, Nanjing, Jiangsu, Peoples R China
4.Michigan State Univ, Dept Math, E Lansing, MI 48824 USA
5.Tel Aviv Univ, Dept Plant Mol Biol & Ecol, George S Wise Fac Life Sci, Tel Aviv, Israel
6.Idaho State Univ, Dept Biol Sci, Pocatello, ID 83209 USA
7.Duke Univ, Dept Biol, Durham, NC USA
8.USDA ARS, Southern Insect Management Res Unit, 141 Expt Stn Rd, Stoneville, MS 38776 USA
9.Weizmann Inst Sci, Dept Biomol Sci, IL-76100 Rehovot, Israel
关键词： Insect sodium channel; Scorpion alpha-toxin; Scorpion beta-toxin; Homology modeling; Mutagenesis; Electrophysiology
期刊名称：INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY （ 影响因子：4.714； 五年影响因子：4.953 ）
ISSN： 0965-1748
年卷期： 2021 年 137 卷
页码：
收录情况： SCI
摘要： Scorpion alpha-toxins bind at the pharmacologically-defined site-3 on the sodium channel and inhibit channel inactivation by preventing the outward movement of the voltage sensor in domain IV (IVS4), whereas scorpion beta-toxins bind at site-4 on the sodium channel and enhance channel activation by trapping the voltage sensor of domain II (IIS4) in its outward position. However, limited information is available on the role of the voltage-sensing modules (VSM, comprising S1-S4) of domains I and III in toxin actions. We have previously shown that charge reversing substitutions of the innermost positively-charged residues in IIIS4 (R4E, R5E) increase the activity of an insect-selective site-4 scorpion toxin, Lqh-dprIT(3)-c, on BgNa(v)1-1a, a cockroach sodium channel. Here we show that substitutions R4E and R5E in IIIS4 also increase the activity of two site-3 toxins, Lqh alpha IT from Leiurusquinquestriatus hebraeus and insect-selective Av3 from Anemonia viridis. Furthermore, charge reversal of either of two conserved negatively-charged residues, D1K and E2K, in IIIS2 also increase the action of the site-3 and site-4 toxins. Homology modeling suggests that S2-D1 and S2-E2 interact with S4-R4 and S4-R5 in the VSM of domain III (III-VSM), respectively, in the activated state of the channel. However, charge swapping between S2-D1 and S4-R4 had no compensatory effects on gating or toxin actions, suggesting that charged residue interactions are complex. Collectively, our results highlight the involvement of III-VSM in the actions of both site 3 and site 4 toxins, suggesting that charge reversing substitutions in III-VSM allosterically facilitate IIS4 or IVS4 voltage sensor trapping by these toxins.
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