通过分裂增强型绿色荧光蛋白互补在细胞中检测到的单纯疱疹病毒糖蛋白gD、gB和gH之间的复合物。
Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein.
作者信息
Avitabile Elisa, Forghieri Cristina, Campadelli-Fiume Gabriella
机构信息
Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo 12, 40126 Bologna, Italy.
出版信息
J Virol. 2007 Oct;81(20):11532-7. doi: 10.1128/JVI.01343-07. Epub 2007 Aug 1.
Abstract
The interactions between herpes simplex virus gD and its nectin1 receptor or between gD, gB, and gH were analyzed by complementation of the N and C portions of split enhanced green fluorescent protein (EGFP) fused to the glycoproteins. The gD(N)-Nect(C) complex was readily detected; the gD(N)-gC(C) complex was undetectable, highlighting the specificity of the assay. Split EGFP complementation was detected between proteins designated gD(N)+gH(C), gD(N)+gB(C), and gH(N)+gB(C)+wtgD (gB was deleted of endocytosis motifs), both in cells transfected with two-tree glycoproteins and in syncytia. The in situ assay provides evidence that gD interacts with gH and gB independently of each other and supports a model whereby gH and gB in complex exert their activities to gD.
摘要
通过将与糖蛋白融合的分裂增强型绿色荧光蛋白（EGFP）的N端和C端进行互补，分析了单纯疱疹病毒gD与其nectin1受体之间或gD、gB和gH之间的相互作用。很容易检测到gD(N)-Nect(C)复合物；而gD(N)-gC(C)复合物则检测不到，这突出了该检测方法的特异性。在转染了两种糖蛋白的细胞以及多核细胞中，在指定的gD(N)+gH(C)、gD(N)+gB(C)和gH(N)+gB(C)+wtgD（gB缺失内吞基序）的蛋白质之间均检测到了分裂EGFP互补。原位检测提供了证据，表明gD与gH和gB相互独立地相互作用，并支持一种模型，即gH和gB形成的复合物对gD发挥其活性作用。
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