Open AccessComplexes between Herpes Simplex Virus Glycoproteins gD, gB, and gH Detected in Cells by Complementation of Split Enhanced Green Fluorescent Protein
Author(s) -
Elisa Avitabile,
Cristina Forghieri,
Gabriella Campadelli-Fiume
Publication year - 2007
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01343-07
Subject(s) - complementation , glycoprotein , biology , herpes simplex virus , herpesvirus glycoprotein b , bimolecular fluorescence complementation , transfection , protein fragment complementation assay , green fluorescent protein , microbiology and biotechnology , syncytium , endocytosis , fluorescence , virology , receptor , virus , biochemistry , gene , viral replication , phenotype , viral entry , physics , quantum mechanics
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 gDN -NectC complex was readily detected; the gDN -gCC complex was undetectable, highlighting the specificity of the assay. Split EGFP complementation was detected between proteins designated gDN +gHC , gDN +gBC , and gHN +gBC +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.