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Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology

机译:埃博拉病毒蛋白GP,NP和VP35对VP40 VLP形态的影响

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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.
机译:最近,我们描述了埃博拉病毒蛋白,NP,GP和VP35在增强VP40 VLP出芽中的作用。为了探讨通过共表达EBOV蛋白导致VP40 VLP芽芽增强而改变VLP结构的可能性,我们进行了密度梯度分析和电子显微镜研究。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的共表达不会显着改变VLP的密度,长度和直径。当NP与VP40共表达时,VLPs的核心出现超微结构变化。总体而言,这些发现表明,在存在GP,NP和/或VP35的情况下,VP40 VLP形态的重大变化可能与VP40 VLP出芽的增加无关。

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