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柑橘衰退病毒p33蛋白通过N端螺旋的自身相互作用。

Self-interaction of Citrus tristeza virus p33 protein via N-terminal helix.

作者信息

Kang Sung-Hwan, Dao Thi Nguyet Minh, Kim Ok-Kyung, Folimonova Svetlana Y

机构信息

University of Florida, Plant Pathology Department, Gainesville, FL 32611, USA.

University of Florida, Plant Pathology Department, Gainesville, FL 32611, USA.

出版信息

Virus Res. 2017 Apr 2;233:29-34. doi: 10.1016/j.virusres.2017.03.008. Epub 2017 Mar 6.

Abstract

Citrus tristeza virus (CTV), the most economically important viral pathogen of citrus, encodes a unique protein, p33. CTV p33 shows no similarity with other known proteins, yet plays an important role in viral pathogenesis: it extends the virus host range and mediates virus ability to exclude superinfection by other variants of the virus. Previously we demonstrated that p33 is an integral membrane protein and appears to share characteristics of viral movement proteins. In this study, we show that the p33 protein self-interacts in vitro and in vivo using co-immunoprecipitation, yeast two hybrid, and bimolecular fluorescence complementation assays. Furthermore, a helix located at the N-terminus of the protein is required and sufficient for the protein self-interaction.

摘要

柑橘衰退病毒(CTV)是柑橘中对经济影响最为重大的病毒病原体,它编码一种独特的蛋白质p33。CTV p33与其他已知蛋白质没有相似性,但在病毒致病过程中发挥着重要作用:它能扩大病毒宿主范围,并介导病毒排除其他病毒变体进行超感染的能力。此前我们证明p33是一种整合膜蛋白,似乎具有病毒运动蛋白的特征。在本研究中,我们通过免疫共沉淀、酵母双杂交和双分子荧光互补分析表明,p33蛋白在体外和体内均能发生自我相互作用。此外,该蛋白质N端的一个螺旋对于蛋白质自我相互作用是必需的且足够了。

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