Author: Fan, Qing; Kopp, Sarah J.; Connolly, Sarah A.; Longnecker, Richard
Title: Structure-Based Mutations in the Herpes Simplex Virus 1 Glycoprotein B Ectodomain Arm Impart a Slow-Entry Phenotype Document date: 2017_5_16
ID: 1v6nf28a_16
Snippet: The gB 3A viruses formed plaques on Vero cells that were 200-fold smaller than WT HSV-1 plaques (Fig. 3A) . Growing the gB 3A virus on Vero cells expressing WT gB (VgB cells) partially rescued the small-plaque phenotype (Fig. 3B) , suggesting that the mutations in gB 3A are responsible for the defect in plaque size. Similarly, complementation with hyperfusogenic gB 876T also restored plaque size (Fig. 7) . Single-step and multistep growth curves .....
Document: The gB 3A viruses formed plaques on Vero cells that were 200-fold smaller than WT HSV-1 plaques (Fig. 3A) . Growing the gB 3A virus on Vero cells expressing WT gB (VgB cells) partially rescued the small-plaque phenotype (Fig. 3B) , suggesting that the mutations in gB 3A are responsible for the defect in plaque size. Similarly, complementation with hyperfusogenic gB 876T also restored plaque size (Fig. 7) . Single-step and multistep growth curves demonstrated a defect in the growth kinetics of the gB 3A viruses (Fig. 4) . Correspondingly, gB 3A viruses took longer than the WT virus to spread through a culture of Vero cells (Fig. 2) . gB 3A protein displays a reduced fusion capacity (Fig. 9A ) that may explain the small-plaque phenotype and delayed growth of the gB 3A viruses.
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