The Cytoplasmic Tail Domain of Epstein-Barr Virus gH Regulates Membrane Fusion Activity through Altering gH Binding to gp42 and Epithelial Cell Attachment

摘要: ABSTRACT Epstein-Barr virus (EBV) is associated with infectious mononucleosis and a variety of cancers as well lymphoproliferative disorders in immunocompromised patients. EBV mediates viral entry into epithelial B cells using fusion machinery composed four glycoproteins: gB, the gH/gL complex, gp42. gB are required for both cell fusion. The specific role has been most elusive among herpesvirus glycoproteins. Previous mutational studies have focused on ectodomain gH not cytoplasmic tail domain (CTD). In this study, we chose to examine function CTD by making serial truncation mutants amino acid substitution determine importance Truncation 8 amino acids (aa 698 706) resulted diminished activity virus-free syncytium formation assay assay. composition was also investigated substitutions that altered hydrophobicity or hydrophilicity CTD. These mutations activity. Interestingly, some hydrophilic lost ability bind gp42 cells. summary, our indicate an important functional domain. IMPORTANCE Infection causes diseases ranging from fairly benign life-threatening cancer. Entry target first step infection cause disease. Understanding mechanism useful development inhibitors developing vaccine approaches. Epithelial main infection. essential glycoproteins include gH/gL, We characterized C-terminal (CTD) panel mutants. found regulates altering attachment. Our may lead better understanding entry, which result novel therapies step.