PDF(Pubmed)
Abstract：
Autophagy serves as a defense mechanism against intracellular pathogens, but several microorganisms exploit it for their own benefit. Accordingly, certain herpesviruses include autophagic membranes into their infectious virus particles. In this study, we analyzed the composition of purified virions of the Epstein-Barr virus (EBV), a common oncogenic γ-herpesvirus. In these, we found several components of the autophagy machinery, including membrane-associated LC3B-II, and numerous viral proteins, such as the capsid assembly proteins BVRF2 and BdRF1. Additionally, we showed that BVRF2 and BdRF1 interact with LC3B-II via their common protein domain. Using an EBV mutant, we identified BVRF2 as essential to assemble mature capsids and produce infectious EBV. However, BdRF1 was sufficient for the release of noninfectious viral envelopes as long as autophagy was not compromised. These data suggest that BVRF2 and BdRF1 are not only important for capsid assembly but together with the LC3B conjugation complex of ATG5-ATG12-ATG15L1 are also critical for EBV envelope release.
摘要：
自噬作为一种防御细胞内病原体的机制，但是一些微生物为了自己的利益而利用它。因此，某些疱疹病毒包括自噬膜进入其感染性病毒颗粒。在这项研究中,我们分析了爱泼斯坦-巴尔病毒（EBV）的纯化病毒体的组成，一种常见的致癌γ-疱疹病毒。在这些中,我们发现了自噬机制的几个组成部分，包括膜相关的LC3B-II，和许多病毒蛋白，例如衣壳组装蛋白BVRF2和BdRF1。此外,我们表明，BVRF2和BdRF1通过它们的共同蛋白结构域与LC3B-II相互作用。使用EBV突变体，我们确定BVRF2对于组装成熟衣壳和产生感染性EBV至关重要。然而,只要自噬不受损，BdRF1就足以释放非感染性病毒包膜。这些数据表明,BVRF2和BdRF1不仅对于衣壳组装是重要的,而且与ATG5-ATG12-ATG15L1的LC3B缀合复合物一起对于EBV包膜释放也是关键的。
