Fig. 8: The VZV gB DIV β30 fold is conserved across the Herpesviridae. | Nature Communications

Fig. 8: The VZV gB DIV β30 fold is conserved across the Herpesviridae.

From: A glycoprotein B-neutralizing antibody structure at 2.8 Å uncovers a critical domain for herpesvirus fusion initiation

Fig. 8

Structure alignments of VZV gB DIV encompassing β-strands 23 and 25–26, and 28–30 with those of HSV (PDB 2GUM), PRV (PDB 6ESC), HCMV (PDB 5C6T), and EBV (PDB 3FVC). The β strands are represented in ribbon format with the side chains shown. The amino acid alignments are shown in the lower right panel with each β-strand highlighted in orange. The consensus sequence (Con) shows conserved residues in upper case with those underlined showing conservations with the exception of one sequence. The red box for the EBV β23 and 25–26 alignment highlights the region not resolved in the crystal structure of 3FVC. Arrow heads highlight the conserved tyrosine (black), conserved ring structure (blue), and conserved charge (red) in β30.

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