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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Ubiquitin-dependent virus particle budding without viral protein ubiquitination
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Ubiquitin-dependent virus particle budding without viral protein ubiquitination

机译：泛素依赖性病毒颗粒出芽而无病毒蛋白泛素化

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摘要

An essential step in the release of an extracellular enveloped virus particle is a budding event that ultimately separates virion and host cell membranes. For many enveloped viruses, membrane fission requires the recruitment of the class E vacuolar protein sorting (VPS) machinery by short, virally encoded peptide sequences termed "late-budding" or "L" domains. Some L-domain peptide sequences (e.g., PSAP) bind directly to components of class E VPS machinery, whereas others (e.g., PPxY) access it indirectly by recruiting ubiquitin ligases. Additionally, ubiquitin itself is known to be generally important for the fission of virion from cellular membranes, and because ubiquitination of cellular transmem-brane proteins can signal the recruitment of class E machinery, a popular model is that deposition of ubiquitin on viral structural proteins mediates class E machinery recruitment. To test this model, we took advantage of a retroviral Gag protein from the prototypic foamy virus (PFV) that is almost devoid of ubiquitin acceptors, and we engineered it to generate extracellular virus-like particles in the complete absence of other viral proteins. Notably, we found that particle budding, induced by a class E VPS machinery-binding L domain (PSAP), proceeded efficiently in the absence of ubiquitin acceptors in PFV Gag. Moreover, when particle release was engineered to be dependent on a viral PPXY motif, the requirement for a catalytically active ubiquitin ligase was maintained, irrespective of the presence or absence of ubiquitin acceptor sites in PFV Gag. Thus, in this model system, ubiquitin conjugation to transacting factors, not viral proteins, appears critical for ubiquitin-dependent enveloped viral particle release.
机译：释放细胞外被膜病毒颗粒的关键步骤是出芽事件，该事件最终将病毒体和宿主细胞膜分开。对于许多包膜病毒，膜裂变需要通过短的，病毒编码的肽序列（称为“晚期”或“ L”结构域）募集E类液泡蛋白分选（VPS）机制。一些L结构域肽序列（例如PSAP）直接结合到E类VPS机械的组件上，而其他L域肽序列（例如PPxY）则通过募集泛素连接酶间接访问它。另外，众所周知，遍在蛋白本身对于病毒颗粒从细胞膜的分裂通常很重要，并且由于细胞跨膜蛋白的遍在蛋白化可以表明E类机器的募集，因此一种流行的模型是遍在蛋白在病毒结构蛋白上的沉积介导E类机械招聘。为了测试该模型，我们利用了原型泡沫病毒（PFV）中几乎没有泛素受体的逆转录病毒Gag蛋白，​​并对其进行了工程改造，以在完全不存在其他病毒蛋白的情况下生成细胞外病毒样颗粒。值得注意的是，我们发现在PFV Gag中不存在泛素受体的情况下，由E类VPS机械结合L结构域（PSAP）诱导的粒子萌芽有效地进行。此外，当将颗粒释放设计为依赖于病毒的PPXY基序时，无论PFV Gag中是否存在泛素受体位点，都对催化活性泛素连接酶的需求得以维持。因此，在该模型系统中，泛素与交易因子而非病毒蛋白的结合对于泛素依赖性包膜病毒颗粒的释放至关重要。

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