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首页> 外文期刊>Applied Microbiology >Minor Coat and Heat Shock Proteins Are Involved in the Binding of Citrus Tristeza Virus to the Foregut of Its Aphid Vector, Toxoptera citricida
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Minor Coat and Heat Shock Proteins Are Involved in the Binding of Citrus Tristeza Virus to the Foregut of Its Aphid Vector, Toxoptera citricida

机译：轻微的涂层和热休克蛋白涉及柑橘Tristeza病毒与其蚜虫载体的前述的结合，毒素孢子虫

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Vector transmission is a critical stage in the viral life cycle, yet for most plant viruses how they interact with their vector is unknown or is explained by analogy with previously described relatives. Here we examined the mechanism underlying the transmission of citrus tristeza virus (CTV) by its aphid vector, Toxoptera citricida , with the objective of identifying what virus-encoded proteins it uses to interact with the vector. Using fluorescently labeled virions, we demonstrated that CTV binds specifically to the lining of the cibarium of the aphid. Through in vitro competitive binding assays between fluorescent virions and free viral proteins, we determined that the minor coat protein is involved in vector interaction. We also found that the presence of two heat shock-like proteins, p61 and p65, reduces virion binding in vitro . Additionally, treating the dissected mouthparts with proteases did not affect the binding of CTV virions. In contrast, chitinase treatment reduced CTV binding to the foregut. Finally, competition with glucose, N -acetyl-β-d-glucosamine, chitobiose, and chitotriose reduced the binding. These findings together suggest that CTV binds to the sugar moieties of the cuticular surface of the aphid cibarium, and the binding involves the concerted activity of three virus-encoded proteins.IMPORTANCE Limited information is known about the specific interactions between citrus tristeza virus and its aphid vectors. These interactions are important for the process of successful transmission. In this study, we localized the CTV retention site as the cibarium of the aphid foregut. Moreover, we demonstrated that the nature of these interactions is protein-carbohydrate binding. The viral proteins, including the minor coat protein and two heat shock proteins, bind to sugar moieties on the surface of the foregut. These findings will help in understanding the transmission mechanism of CTV by the aphid vector and may help in developing control strategies which interfere with the CTV binding to its insect vector to block the transmission.
机译：矢量传输是病毒生命周期的关键阶段，但对于大多数植物病毒，它们如何与其载体相互作用未知，或者通过与先前描述的亲属类似的类比解释。在这里，我们通过其蚜虫载体，Toxoptera Citricida检测了柑橘Tristeza病毒（CTV）的潜在机制，目的是鉴定它用于与载体相互作用的病毒编码的蛋白质。使用荧光标记的病毒粒子，我们证明了CTV特异性结合蚜虫的纤维纤维的衬里。通过在荧光病毒藻和游离病毒蛋白之间的体外竞争性结合测定，我们确定次胶片蛋白参与载体相互作用。我们还发现，两种热冲击样蛋白，P61和P65的存在降低了体外病毒素结合。另外，用蛋白酶治疗解剖的嘴巴不影响CTV病毒粒子的结合。相反，几丁酶治疗将CTV与前述有结合减少。最后，用葡萄糖，N-acetyl-β-D-葡糖胺，千核糖和赤藓糖发育的竞争降低了结合。这些发现表明，CTV与蚜虫纤维化的内表面的糖部分结合，结合涉及三种病毒编码的蛋白质的协调活性。分析有限的信息是关于柑橘三分肠病毒和其蚜虫之间的特异性相互作用所知的有限信息vectors。这些互动对于成功传播过程很重要。在这项研究中，我们将CTV保留部位定位为蚜虫前肠的纤维化。此外，我们证明了这些相互作用的性质是蛋白质 - 碳水化合物结合。病毒蛋白，包括次要涂层蛋白和两个热休克蛋白，与前述表面的糖部分结合。这些发现将有助于理解蚜虫载体的CTV的传动机制，并且可以帮助开发干扰与其昆虫载体的CTV结合以阻挡传输的控制策略。

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