Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B.

ABSTRACT: Herpes simplex virus glycoprotein B (gB) is one of four glycoproteins essential for viral entry and cell fusion. Recently, an x-ray structure of the nearly full-length trimeric gB ectodomain was determined. Five structural domains and two linker regions were identified in what is probably a postfusion conformation. To identify functional domains of gB, we performed random linker-insertion mutagenesis. Analyses of 81 mutants revealed that only 27 could fold to permit processing and transport of gB to the cell surface. These 27 mutants fell into three categories. Insertions into two regions excluded from the solved structure (the N terminus and the C-terminal cytoplasmic tail) had no negative effect on cell fusion and viral entry activity, identifying regions that can tolerate altered struct

SUBMITTER: Lin E 

PROVIDER: S-EPMC1941792 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature