Self-interaction of ORF II protein through the leucine zipper is essential for Soybean chlorotic mottle virus infectivity.
Self-interaction of ORF II protein through the leucine zipper is essential for Soybean chlorotic mottle virus infectivity.
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DOI：
10.1016/j.virol.2004.11.026
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发表时间：
2005-02
期刊：
影响因子：
3.7
通讯作者：
Y. Takemoto;T. Hibi
中科院分区：
文献类型：
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作者：
Y. Takemoto;T. Hibi
大豆褪绿斑驳病毒（SbCMV）的ORF II蛋白（PII）是病毒生活史中必需的蛋白。我们研究了SbCMV PII与自身的相互作用，并与其他必要的病毒蛋白质使用Gal 4为基础的酵母双杂交系统。PII仅与自身相互作用，不与任何其他病毒蛋白相互作用。PII-PII相互作用通过基于Sos的酵母双杂交系统和far-western分析证实。缺失诱变将自相互作用结构域定位到C-末端48个氨基酸（氨基酸154-201），其含有两个推定的亮氨酸拉链基序。在拉链序列中引入亮氨酸/异亮氨酸的氨基酸取代防止了PII-PII相互作用并消除了SbCMV的感染性。这些结果表明，PII通过亮氨酸拉链的自我相互作用对于病毒感染是必要的。
The ORF II protein (PII) of Soybean chlorotic mottle virus (SbCMV) is essential for the virus life cycle. We investigated the interactions of SbCMV PII with itself and with other essential virus proteins using a Gal4-based yeast two-hybrid system. PII interacted only with itself and not with any other virus proteins. The PII–PII interaction was confirmed by a Sos-based yeast two-hybrid system and a far-western analysis. Deletion mutagenesis mapped the self-interacting domain to the C-terminal 48 amino acids (amino acids 154–201), which contain two putative leucine zipper motifs. Introduction of amino acid substitutions to leucine/isoleucine in zipper sequences prevented the PII–PII interaction and abolished the infectivity of SbCMV. These results revealed that the self-interaction of PII through a leucine zipper is necessary for virus infection.