Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.
Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19798-803. doi: 10.1073/pnas.1212900109. Epub 2012 Nov 12.
Glycoprotein E (gE) of HSV plays a key role in cell-to-cell spread and virus-induced cell fusion. Here, we report that this function of gE requires the cooperation of tegument proteins UL11, UL16, and UL21. We found that the four proteins come together with very high efficiency to form a complex in transfected cells and in a manner that is regulated and coordinated. In particular, the inefficient interaction of UL16 with each membrane protein (UL11 and gE) observed in pairwise transfections became efficient when other binding partners were present. The significance of these interactions was revealed in studies of viral mutants, which showed that each of these tegument proteins is critical for processing, transport, and biological activity of gE. These findings provide insights into the mechanisms of how gE executes its function and also have implications in understanding HSV assembly and budding.
单纯疱疹病毒糖蛋白 E (gE) 在细胞间传播和病毒诱导的细胞融合中起着关键作用。在这里，我们报告称，gE 的这一功能需要包膜蛋白 UL11、UL16 和 UL21 的合作。我们发现这四种蛋白在转染细胞中以非常高的效率聚集在一起形成复合物，并且这种聚集受到调控和协调。特别是，在成对转染中观察到 UL16 与每种膜蛋白 (UL11 和 gE) 的低效相互作用，当存在其他结合伴侣时，这种相互作用变得高效。这些相互作用的意义在病毒突变体的研究中得到了揭示，这些研究表明，这些包膜蛋白中的每一种对于 gE 的加工、运输和生物学活性都是至关重要的。这些发现为了解 gE 如何执行其功能提供了深入的认识，也为理解单纯疱疹病毒的组装和出芽提供了启示。
