Related Experiment Video
Updated: Jul 13, 2026
Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
Published on: September 10, 2020
Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split
Elisa Avitabile1, Cristina Forghieri, Gabriella Campadelli-Fiume
1Department of Experimental Pathology, Section on Microbiology and Virology, University of Bologna, Via San Giacomo 12, 40126 Bologna, Italy.
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.
