Complexes Between Herpes Simplex Virus Glycoproteins GD, GB, and GH Detected in Cells by Complementation of Split Enhanced Green Fluorescent Protein

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 2007 Aug 3

PMID 17670828

Citations 80

Authors

Elisa Avitabile

Cristina Forghieri

Gabriella Campadelli-Fiume

Affiliations

Soon will be listed here.

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.

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