Fig. 5: Glycan shielding of the gB apex, leaving DI and DIV unencumbered.
From: Prefusion structure, evasion and neutralization of HSV-1 glycoprotein B
a, Identification of N-linked glycans on the prefusion gB structure, highlighting the cryo-EM reconstruction density for several of these glycans. Labels are provided for glycans on a single protomer. b,c, Prefusion gB N-linked glycan coverage, as determined by molecular dynamics simulation, depicted by structure (b) and sequence (c). In c, green, magenta and cyan represent glycan shielding, refolding regions and non-refolding regions, respectively. N-linked glycans shield the gB apex and occlude refolding regions outside of DV. d, Sites of N-linked glycosylation in HSV-1 gB, coloured green if conserved or grey if absent in three other common alphaherpesviruses: HSV-2, HHV-3 and pseudorabies virus (PRV). e, Heatmap showing the degree of total residue masking related to residue-level correspondence between refolding regions, surface exposure and glycan shielding. The heatmap is coloured from white (0% of total residues are masked) to dark green (50% of total residues are masked). For domain interface residues, three of 20 (15%) are shielded in non-refolding regions and 23 of 47 (49%) are shielded in refolding regions. For non-domain interface residues, 79 of 460 (17%) are shielded in non-refolding regions and five of 33 (15%) are shielded in refolding regions. Of note, refolding regions at domain interfaces are the most highly masked by glycans.
