Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: Facilitated trafficking to the inner nuclear membrane
Trafficking of ODV-E66 is mediated via a sorting motif and other viral proteins: Facilitated trafficking to the inner nuclear membrane
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DOI：
10.1073/pnas.0402727101
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发表时间：
2004-06-01
影响因子：
11.1
通讯作者：
Summers, MD
中科院分区：
文献类型：
--
作者：
Braunagel, SC;Williamson, ST;Summers, MD
包膜蛋白ODV-E66的N-末端33足以在苜蓿银纹夜蛾核型多角体病毒感染期间将融合蛋白运输至核内膜和ODV包膜。该序列具有两个不同的特征：（i）18 as的极疏水序列和（ii）靠近疏水序列的C末端的带正电荷的氨基酸。在没有感染的情况下，该序列足以促进蛋白质在内核膜处的积累。共价交联的结果表明，在从内质网到核膜的运输过程中，基序的赖氨酸接近FP 25 K和/或BV/ODV-E26。我们建议，33作为包括一个签名，用于分选蛋白质的内核膜（分选基序），并且，与其他居民蛋白质的内核膜，ODV-E66和分选基序融合不随机扩散，从其网站的插入在内质网的核膜和病毒诱导的核内膜。相反，在感染过程中，运输是由蛋白质-蛋白质相互作用介导的。
The N-terminal 33 as of the envelope protein ODV-E66 are sufficient to traffic fusion proteins to intranuclear membranes and the ODV envelope during infection with Autographa californica nucleopolyhedrovirus. This sequence has two distinct features: (i) an extremely hydrophobic sequence of 18 as and (ii) positively charged amino acids close to the C-terminal end of the hydrophobic sequence. In the absence of infection, this sequence is sufficient to promote protein accumulation at the inner nuclear membrane. Covalent cross-linking results show that the lysines of the motif are proximal to FP25K and/or BV/ODV-E26 during transit from the endoplasmic reticulum to the nuclear envelope. We propose that the 33 as comprise a signature for sorting proteins to the inner nuclear membrane (sorting motif) and that, unlike other resident proteins of the inner nuclear membrane, ODV-E66 and sorting-motif fusions do not randomly diffuse from their site of insertion at the endoplasmic reticulum to the nuclear envelope and viral-induced intranuclear membranes. Rather, during infection, trafficking is mediated by protein-protein interactions.