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_4
Snippet: Our previous mutagenesis study demonstrated that fusion was impaired by mutations in the domain V arm that were predicted to disrupt the coil-arm interaction (20) . This phenotype could be rescued by the addition of a hyperfusogenic mutation in the gB cytoplasmic tail, suggesting that the reduced fusion phenotype was not due to global misfolding. When three alanine substitutions were made simultaneously in the gB arm (I671A, H681A, and F683A; gB .....
Document: Our previous mutagenesis study demonstrated that fusion was impaired by mutations in the domain V arm that were predicted to disrupt the coil-arm interaction (20) . This phenotype could be rescued by the addition of a hyperfusogenic mutation in the gB cytoplasmic tail, suggesting that the reduced fusion phenotype was not due to global misfolding. When three alanine substitutions were made simultaneously in the gB arm (I671A, H681A, and F683A; gB 3A here), fusion was greatly reduced in a cell-cell fusion assay. If the interaction of the arm with the coil contributes to the conversion from a prefusion to a postfusion form, the gB 3A mutations may energetically favor the prefusion state of gB.
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