首页> 美国卫生研究院文献>Journal of Venom Research >Entomotoxicity of jaburetox: revisiting the neurotoxic mechanisms in insects
【2h】

Entomotoxicity of jaburetox: revisiting the neurotoxic mechanisms in insects

机译:jaburetox的昆虫毒性:重新审视昆虫的神经毒性机制

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务,本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文,但由于OA文献来源多样且变更频繁,仍可能出现获取不到、文献不完整或与标题不符等情况,如果获取不到我们将提供退款服务。请知悉。

摘要

Ureases are metalloenzymes that hydrolyze urea to ammonia and carbamate. The main urease isoforms present in the seeds of Canavalia ensiformis (jack bean urease – JBU and canatoxin) exert a variety of biological activities. The insecticidal activity of JBU is mediated, at least in part, by jaburetox (Jbtx), a recombinant peptide derived from the JBU amino acid sequence. In this article, we review the neurotoxicity of Jbtx in insects. The insecticidal activity of Jbtx has been investigated in a variety of insect orders and species, including Blattodea (the cockroaches Blatella germânica, Nauphoeta cinerea, Periplaneta americana e Phoetalia pallida), Bruchidae (Callosobruchus maculatus – cowpea weevil), Diptera (Aedes aegypti – mosquito), Hemiptera (Dysdercus peruvianus – cotton stainer bug; Oncopeltus fasciatus – large milkweed bug, and the kissing bugs Rhodnius prolixus and Triatoma infestans), Lepidoptera (Spodoptera frugiperda – fall army worm) and Orthoptera (Locusta migratoria – locust). In N. cinerea, the injection of Jbtx induces marked alteration of locomotor and grooming behavior, whereas in T. infestans Jbtx causes leg paralysis, an extension of the proboscis and abnormal antennal movements. Electromyographical analysis showed that Jbtx causes complete neuromuscular blockade in P. pallida. The same treatment in N. cinerea and L. migratoria causes a decrease in the action potential firing rate. Jbtx forms membrane pore-channels compatible with cations in bilipid membranes. A study using B. germanica voltage-gated sodium (Nav1.1) channels that were heterologously expressed in Xenopus laevis oocytes correlated the entomotoxicity of Jbtx with the activation of these channels. Taken together, these findings demonstrate the potential of this peptide as a natural pesticide.
机译:令人兴保酶是金属酶,即水解尿素至氨和氨基甲酸酯。存在于CanaviaLia ensiformis的种子中的主要脲酶同种型(Jack Bean脲酶 - JBU和Canatoxin)施加各种各样的生物活动。 JBU的杀虫活性至少部分地由Jaburetox(JBTX),衍生自JBU氨基酸序列的重组肽。在本文中,我们审查了昆虫中JBTX的神经毒性。 JBTX的杀虫活性已经在各种昆虫订单和物种中进行了调查,包括Blattodea(蟑螂BlatellaGermânica,Nauphoeta Cinerea,Periplaneta Americana E菲特纳Pallida),Bruchidae(Callosobruchus Maculatus - Cowpea Weevil),Diptera(Aedes Aegypti - 蚊子),半翅目(Dysdercus Peruvianus - 棉花染色体虫; Oncopeltus fasciatus - 大乳草虫,以及亲吻虫子rhodnius proLixus和Triatoma infestans),鳞翅目(Spodoptera frugiperda - 北陆军蠕虫)和北方术士(洛卡斯州普罗瓦氏症 - 蝗虫)。在N.Cinerea中,JBTX的注入诱导了机器人和美容行为的标记改变,而In Infestans JBTX会导致腿瘫痪,延长长期和异常抵抗运动。肌电图分析表明,JBTX导致P. Pallida中完全神经血清障碍。在N. Cinerea和L.Migratoria的同一治疗方法导致动作潜在的射击率降低。 JBTX形成膜孔通道与Bilipid膜中的阳离子兼容。使用B.Greganica电压门控钠(Nav1.1)在Xenopus Laevis卵母细胞中异源表达的钠(Nav1.1)通道与这些通道的激活相关相关的jbtx的昆虫毒性。在一起,这些研究结果证明了这种肽作为天然农药的潜力。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号