Non-polar distribution of green fluorescent protein on the surface of Autographa californica nucleopolyhedrovirus using a heterologous membrane anchor
Non-polar distribution of green fluorescent protein on the surface of Autographa californica nucleopolyhedrovirus using a heterologous membrane anchor
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DOI：
10.1016/s0168-1656(02)00023-8
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发表时间：
2002-05-23
影响因子：
4.1
通讯作者：
Jones, IM
中科院分区：
文献类型：
--
作者：
Chapple, SDJ;Jones, IM
将展示蛋白与 AcMNPV 主要包膜糖蛋白 gp64 融合后，异源蛋白可展示在芽纹苜蓿银纹夜蛾核多角体病毒 (AcMNPV) 的表面上。然而，显示仅限于病毒体的两极，并且水平相对较低。为了研究与病毒表面展示兼容的替代膜锚序列的使用，我们构建了一个包含 gp64 信号肽和来自水泡性口炎病毒 (VSV) G 糖蛋白的膜锚的展示载体。在这些信号之间引入编码绿色荧光蛋白（GFP）的基因，导致昆虫细胞表面和重组芽生病毒颗粒上大量展示 GFP。此外，与基于 gp64 的融合蛋白相比，GFP 定位于病毒颗粒的侧表面。 (C) 2002 Elsevier Science B.V. 保留所有权利。
Heterogeneous proteins can be displayed on the surface of the budded form of Autographa californica nucleopolyhedrovirus (AcMNPV) after fusion of the display protein to the AcMNPV major envelope glycoprotein, gp64. However, display is restricted to the poles of the virion and is relatively low level. To investigate the use of alternative membrane anchor sequences that would be compatible with virus surface display, we have constructed a display vector containing the gp64 signal peptide and a membrane anchor from the vesicular stomatitis virus (VSV) G glycoprotein. Introduction of a gene encoding green fluorescent protein (GFP) between these signals led to abundant display of GFP on the surface of insect cells and on recombinant budded virions. In addition, and in contrast to gp64 based fusion proteins, GFP was localized to the lateral virion surfaces. (C) 2002 Elsevier Science B.V. All rights reserved.