Rice Stripe Tenuivirus Nonstructural Protein 3 Hijacks the 26S Proteasome of the Small Brown Planthopper via Direct Interaction with Regulatory Particle Non-ATPase Subunit 3
Rice Stripe Tenuivirus Nonstructural Protein 3 Hijacks the 26S Proteasome of the Small Brown Planthopper via Direct Interaction with Regulatory Particle Non-ATPase Subunit 3
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稻条细病毒非结构蛋白 3 通过与调节颗粒非 ATP 酶亚基 3 直接相互作用劫持小褐飞虱的 26S 蛋白酶体
DOI：
10.1128/jvi.03055-14
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发表时间：
2015-02
影响因子：
5.4
通讯作者：
Zhou, Xueping
中科院分区：
文献类型：
--
作者：
Fu, Shuai;Li, Chenyang;Zhu, Zeng-Rong;Zhou, Xueping
摘要泛素/26 S蛋白酶体系统在调节宿主防御病原体的过程中起着重要作用。以前的研究已经强调了泛素/26 S蛋白酶体在哺乳动物和植物病毒感染期间的防御中的不同作用，但它们在传播这些病毒的载体中的作用仍不清楚。在这项研究中，我们确定了26 S蛋白酶体存在于小褐飞虱（SBPH）（灰飞虱），并具有类似于植物和哺乳动物的成分。水稻条纹病毒（Rice stripe virus，RSV）26 S蛋白酶体破坏后，在传播载体SBPH中的积累量增加，表明SBPH 26 S蛋白酶体通过调控RSV的积累而发挥防御RSV感染的作用。酵母双杂交分析确定，26 S蛋白酶体的一个亚基，命名为RPN 3，可以与RSV NS 3相互作用。RPN 3的瞬时过表达对RSV NS 3的RNA沉默抑制活性没有影响。然而，NS 3可以抑制SBPH rpn 3补充酵母中的rpn 3突变的能力。我们的研究结果还表明，RPN 3和NS 3之间的直接相互作用是负责抑制RPN 3的互补能力。在体内，我们发现在SBPH组织中的RSV滴度高的泛素化蛋白的积累，和沉默的rpn 3导致SBPH蛋白酶体介导的蛋白水解功能障碍。因此，RPN 3被抑制的含病毒SBPH由于RSV的更高积累而更有效地传播病毒。我们的研究结果表明，RSV NS 3蛋白能够通过与RPN 3亚基的直接相互作用来劫持SBPH中的26 S蛋白酶体，以减弱宿主的防御反应。重要性我们表明，第一次，26 S蛋白酶体成分存在于小褐飞虱，并在防御其载体植物病毒（RSV）中发挥作用。反过来，RSV编码一种蛋白质，该蛋白质通过与26 S蛋白酶体亚基RPN 3直接相互作用破坏SBPH 26 S蛋白酶体。我们的研究结果表明，在植物宿主中观察到的分子军备竞赛可以扩展到传播这些病毒的昆虫载体。
ABSTRACT The ubiquitin/26S proteasome system plays a vital role in regulating host defenses against pathogens. Previous studies have highlighted different roles for the ubiquitin/26S proteasome in defense during virus infection in both mammals and plants, but their role in the vectors that transmit those viruses is still unclear. In this study, we determined that the 26S proteasome is present in the small brown planthopper (SBPH) (Laodelphgax striatellus) and has components similar to those in plants and mammals. There was an increase in the accumulation of Rice stripe virus (RSV) in the transmitting vector SBPH after disrupting the 26S proteasome, indicating that the SBPH 26S proteasome plays a role in defense against RSV infection by regulating RSV accumulation. Yeast two-hybrid analysis determined that a subunit of the 26S proteasome, named RPN3, could interact with RSV NS3. Transient overexpression of RPN3 had no effect on the RNA silencing suppressor activity of RSV NS3. However, NS3 could inhibit the ability of SBPH rpn3 to complement an rpn3 mutation in yeast. Our findings also indicate that the direct interaction between RPN3 and NS3 was responsible for inhibiting the complementation ability of RPN3. In vivo, we found an accumulation of ubiquitinated protein in SBPH tissues where the RSV titer was high, and silencing of rpn3 resulted in malfunction of the SBPH proteasome-mediated proteolysis. Consequently, viruliferous SBPH in which RPN3 was repressed transmitted the virus more effectively as a result of higher accumulation of RSV. Our results suggest that the RSV NS3 protein is able to hijack the 26S proteasome in SBPH via a direct interaction with the RPN3 subunit to attenuate the host defense response. IMPORTANCE We show, for the first time, that the 26S proteasome components are present in the small brown planthopper and play a role in defense against its vectored plant virus (RSV). In turn, RSV encodes a protein that subverts the SBPH 26S proteasome via direct interaction with the 26S proteasome subunit RPN3. Our results imply that the molecular arms race observed in plant hosts can be extended to the insect vector that transmits those viruses.
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影响因子：
7.4
作者：
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通讯作者：
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影响因子：
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作者：
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影响因子：
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作者：
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通讯作者：
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