Fig. 4 | Nature Communications

Fig. 4

From: Structural basis of respiratory syncytial virus subtype-dependent neutralization by an antibody targeting the fusion glycoprotein

Fig. 4

Arg or Lys at position 201 is critical for RSV F recognition and neutralization by 5C4. ad Fractional binding of mAbs 5C4 (black bars) and D25 (white bars) to DS-Cav1–stabilized pre-F variants relative to motavizumab. a Binding to A-chimera constructs (RSV A2 pre-F variants). b Binding to B-chimera constructs (RSV B18537 pre-F variants). c Binding to RSV A2 pre-F position 201 variants. d Binding to RSV B strain 18537 pre-F position 201 variants. Bars represent the standard relative fractional binding of three replicates with error bars indicating standard deviation. P values calculated using two-way ANOVA are shown with symbols, where ns is P > 0.05, **P ≤ 0.01, ***P ≤ 0.001 and ****P ≤ 0.0001. e, f Neutralization activity of 5C4 against subtype A strain A2 and subtype B strain 18537 with and without subtype-specific substitutions at position 201. e The EC50 of 5C4 against A2 wild-type and K201N-mutated virus is 0.004±0.0008 μg/mL (Mean±SD) and 0.41±0.11 μg/mL, respectively, from three independent experiments. f The EC50 of 5C4 against RSV B strain 18537 wild-type and N201K-mutated virus is 9.149±0.056 μg/mL and 0.022±0.003 μg/mL, respectively. Data are representative from three independent experiments

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