Johnson Reed F, Bell Peter, Harty Ronald N
Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, 3800 Spruce St,, Philadelphia, PA 19104, USA.
Virol J. 2006 May 23;3:31. doi: 10.1186/1743-422X-3-31.
Recently we described a role for Ebola virus proteins, NP, GP, and VP35 in enhancement of VP40 VLP budding. To explore the possibility that VLP structure was altered by co-expression of EBOV proteins leading to the observed enhancement of VP40 VLP budding, we performed density gradient analysis as well as electron microscopy studies. Our data suggest that VP40 is the major determinant of VLP morphology, as co-expression of NP, GP and VP35 did not significantly change VLP density, length, and diameter. Ultra-structural changes were noted in the core of the VLPs when NP was co-expressed with VP40. Overall, these findings indicate that major changes in morphology of VP40 VLPs were likely not responsible for enhanced budding of VP40 VLPs in the presence of GP, NP and/or VP35.
最近，我们阐述了埃博拉病毒蛋白NP、GP和VP35在增强VP40病毒样颗粒（VLP）出芽方面的作用。为了探究埃博拉病毒（EBOV）蛋白的共表达是否会改变VLP结构，进而导致观察到的VP40 VLP出芽增强，我们进行了密度梯度分析以及电子显微镜研究。我们的数据表明，VP40是VLP形态的主要决定因素，因为NP、GP和VP35的共表达并未显著改变VLP的密度、长度和直径。当NP与VP40共表达时，在VLP的核心部位发现了超微结构变化。总体而言，这些发现表明，在存在GP、NP和/或VP35的情况下，VP40 VLP形态的主要变化可能并非VP40 VLP出芽增强的原因。
