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Figure 1

From: A cocktail of human monoclonal antibodies broadly neutralizes North American rabies virus variants as a promising candidate for rabies post-exposure prophylaxis

Figure 1

RAB2 and R172 binding and neutralization of rabies glycoproteins. (a) Schematic of rabies glycoprotein showing non-overlapping antigenic site locations of RAB1 (antigenic site III) and RAB2 (antigenic site II), figure was created with BioRender.com. (b) RAB2 recognition of antigenic site II alanine mutants. Each amino acid in the antigenic site II of ERA full length surface glycoprotein (a.a. 1–524) was substituted with alanine by site directed mutagenesis. (c) ELISA binding of RAB2 to the wild-type ERA439 or RAB1 escape N336D R346K and RAB2 escape E33K mutants. (d) Affinity measurement of RAB2 antibody against wild type ERA439, conducted by Bio-layer interferometry. (e) ELISA binding of R172 to the wild-type ERA439 or RAB1 escape N336D R346K and RAB2 escape E33K mutants. (f–h) R172 pseudovirus neutralization against lentivirus bearing the wild-type ERA glycoprotein (f), E33K (g) and N336D R346K (h) mutants. ERA glycoprotein was used as backbone to introduce all mutants. EC50 values were calculated by nonlinear regression analysis using Prism version 8.1.1. Data is plotted as the mean ± s.d. from n = 4 independent experiments.

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