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. 2013 Jan 7;8(1):e53273. doi: 10.1371/journal.pone.0053273

Figure 1. LCM virus glycoprotein overview.

Figure 1

(A) Schematic view of the glycoprotein and localization of the N-glycosylation site mutations. The signal peptide SSP in grey (aa 1–58), the precursor glycoprotein GPC (aa 59–498), the subunits GP1 in blue (aa 59–265) and GP2 in green (aa266–498) containing the transmembrane anchor (aa 439–456, black) are shown. The eleven conserved N-glycosylation sites across arenaviruses are represented. Mutations leading to: (i) deletion of N-glycan on LCM virus in black, (ii) addition of N-glycan on LCM virus in grey. (B) Modified crystal structure of Machupo virus GP1. Residues in direct interaction with human transferrin receptor 1 are shown in magenta. Positions of N-linked glycans conserved by both LCMV and Machupo virus are purple. Those conserved only by LCMV are red and those conserved only by Machupo are blue. (C) Crystal structure of LCMV GP2 ectodomain. Positions of the glycosylated asparagines from consensus sequence are shown in red (8–11). (D) Crystal of Machupo virus GP1 (Light cyan) superimposed on receptor bound Machupo GP1 (Light pink) with glycan 2 shown in cyan and magenta, respectively.