Fig. 2: Crystal structure of Sin Nombre GnH in complex with Fab SNV-42.

a, Structure of the Gn–Fab complex. The Fab is displayed with the backbone of the light and heavy chains coloured light grey or dark grey, respectively. The CDR loops are thicker and coloured according to the key in c. The Gn is displayed as a ribbon diagram with each of the three domains coloured according to the key in c. The two N-linked glycosylation sites are displayed in green and the location of the two previously described escape mutants (T312K and K357Q) are displayed in orange. Inset is a zoomed panel of the binding site with the side chains of the two escape mutant residues displayed. b, The backbone of the SNV Gn^H in pink overlaid on several previously reported Gn^H crystal structures from different hantavirus species in grey. These include Andes orthohantavirus (PDB ID 6Y5F), Maporal orthohantavirus (PDB ID 6Y62), Puumala orthohantavirus (PDB ID 5FXU) and Hantaan orthohantavirus (PDB ID 5OPG). Of note is the capping loop, indicated, which was replaced in SNV Gn^H with a much shorter GGSG linker to aid crystallogenesis. c, A domain schematic of the Sin Nombre glycoprotein precursor protein that is cleaved at the WAASA cleavage site to form Gn and Gc. The crystallized Gn^H region is outlined in bold and coloured according to domain. Transmembrane regions are displayed in dark grey and N-linked glycosylation sites displayed in green. The sequence of the capping loop between residues 86–99 is displayed alongside the shorter GGSG linker that has been used in its place for this experiment.