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. 2021 Apr 21;218(6):e20200303. doi: 10.1084/jem.20200303

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© 2021 Lanz et al.

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Figure 5. — IFITM3 sensitizes IAV to antibody-mediated neutralization in vivo. (a) Predicted inhibition curves of antibodies interfering with IAV binding to host cells for IAV with regular trimer number (300 trimers/virion, black line) and reduced trimer numbers (reduction to 80%, 73%, 60%, and 40% HA content, red lines). (b) Predicted replicative fitness of IAV with regular trimer number (300 trimers/virion, black line) and reduced trimer numbers (reduction to 80%, 73%, 60%, and 40% HA content, red lines) as a function of antibody concentrations. Modeling was performed for antibodies inhibiting virus binding to host cells. (c) Predicted virus dynamics in the presence of antibodies acting on the stage of binding for virus stocks with and without IFITM3 incorporation. The antibody concentration was chosen such that the fitness difference for virus stocks with and without IFITM3 incorporation is maximal. (d) Morbidity after lethal challenge with PR8 virus (80 PFU) in the presence of a low dose of a PR8 HA head-specific monoclonal antibody (0.375 mg/kg) or a control antibody. Error bars represent SD. Statistically significant differences due to the absence of IFITM3 in mice that received PR8 HA head-specific antibody treatment (n = 7–9 mice/group) were assessed by two-way ANOVA with repeated measures. *, P < 0.05; **, P < 0.01. (e) Lung virus titers at 6 d after infection with PR8 virus are reduced by a low dose of a PR8 HA head-specific monoclonal antibody in WT but not in IFITM3 knockout mice (n = 3–4 mice/group). Error bars represent SD. Statistical significance was assessed by a one-sided Wilcoxon rank sum test. Note that with sample sizes of three data points per group, the smallest P value possible in a Wilcoxon rank sum test is P = 0.05.