Multiple sequence alignment of gB homologs.

<p>Protein sequence alignment of HCMV (strain AD169), EBV (strain B958), and HSV-1 (strain KOS) (UniProtKB accession numbers P06473, Q777B0, P06437, respectively) was generated and analyzed using ClustalW2 [<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1005227#ppat.1005227.ref032" target="_blank">32</a>] and ESPript 3.x [<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1005227#ppat.1005227.ref033" target="_blank">33</a>]. The secondary structure of HCMV is displayed above the alignment and the secondary structure of HSV-1 (2GUM) [<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1005227#ppat.1005227.ref016" target="_blank">16</a>] is displayed below the alignment. Secondary structure elements are colored by domain, as in <a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1005227#ppat.1005227.g001" target="_blank">Fig 1</a>. Unresolved residues are denoted with dashed lines, signal sequences as orange letters and residues in fusion loops as blue letters. Cysteines participating in disulfide bonds are highlighted in green, furin cleavage sites, in pink, glycosylation sites, in cyan. First residue in the crystallized HCMV gB construct is highlighted in brown. Identical residues are shown as white text on red background, similar residues are shown as red text.