Fig. 1: RABV G recognition by RVC20. | Nature Communications

Fig. 1: RABV G recognition by RVC20.

From: Structure of the prefusion-locking broadly neutralizing antibody RVC20 bound to the rabies virus glycoprotein

Fig. 1: RABV G recognition by RVC20.The alternative text for this image may have been generated using AI.

a Domain organization of RABV G (top row) as inferred by homology to VSV G10, and design of the recombinant domain III construct for structure determination (bottom row). Hatched fields in the construct denote unresolved regions in the X-ray structure. β strands are shown as arrows labeled in lower case in accordance with the VSV G structure10. TM transmembrane region, ST Strep tag. b Crystal structure of the complex between RABV G domain III and the RVC20 scFv. The variable domain of the heavy chain (VH) is shown in green, the variable domain of the kappa light chain (VK) is shown in white and the antigen is shown in orange. The CDRs of the mAb and the β strands and disulfide bonds of the antigen are labeled. c Sequence conservation of the tripartite epitope. The RABV G sequence is displayed as a sequence logo, indicating the conservation per residue across 1412 unique full-length RABV G sequences in GenBank (details are listed in Table 2). The color-coded bar chart shows the BSA per RABV G residue in the complex contributed by heavy chain (green) and light chain (white) residues. h, hydrogen bond involved; s, salt bridge involved. Differences in epitope sequence across the Lyssavirus genus are shown below, with the corresponding neutralizing potency of RVC20 qualitatively summarized to the right9: ++, strong; +, attenuated; −, not detected; +/−, isolate-dependent; nd, not determined. d Detail of the interaction interface. Residues on both sides of the interface are labeled and are shown as sticks with oxygen atoms in red and nitrogen atoms in blue. Secondary-structure elements and disulfide bonds are labeled as in b. e Neutralization of recombinant RABV mutants with mAb RVC20 on BSR cells 48 h after infection; n = 3 independent experiments. f Neutralization of wild-type and mutant Lagos bat virus G-pseudotyped lentiviruses with mAb RVC20 on BHK-21 cells 72 h after infection. LOD, limit of detection; n = 2 independent experiments. Data are displayed as means ± s.d. Statistical analysis was performed using Tukey’s test with α = 0.05. ****P < 0.0001; ***P < 0.001; *P < 0.05; ns, not significant (P > 0.05). Source data are provided as a Source Data file.

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