Fig. 3: The NA D113A mutation provides no advantage for virus growth in SAE cells but increases NA thermostability and sialidase activity under Ca2+ -depleted conditions. | Communications Biology

Fig. 3: The NA D113A mutation provides no advantage for virus growth in SAE cells but increases NA thermostability and sialidase activity under Ca2+ -depleted conditions.

From: Modulation of human-to-swine influenza a virus adaptation by the neuraminidase low-affinity calcium-binding pocket

Fig. 3

a Viral growth kinetics of sOH/04 (blue), hVIC/11 (yellow), hVIC/11-A138S(red), hVIC/11-D113A (black), and hVIC/11-A138S/D113A (purple) in MDCK, PK15, A549, HAE, and SAE cells infected at an MOI of 0.01. A mock control (white) is included. Values represent the mean ± SD of three independent experiments. p values were obtained by ordinary one-way ANOVA. b Thermostability of sOH/04 (blue), hVIC/11 (yellow), hVIC/11-A138S(red), hVIC/11-D113A (black), hVIC/11-A138S/D113A (purple) NAs determined in presence (solid line) or absence (dashed line) of Ca2+. c T50 was obtained by adjusting the data to a dose-response variable slope nonlinear fit and values are shown as the means of three independent experiments. p values were obtained by ordinary one-way ANOVA. d NA sialidase activity of sOH/04 (blue), hVIC/11 (yellow), hVIC/11-A138S(red), hVIC/11-D113A (black), and hVIC/11-A138S/D113A (purple) at 0 mM Ca2+ expressed as a percentage of the reaction velocity compared to 2 mM Ca2+ (100% NA activity) at 37 °C. Values represent the means ± SD of three independent experiments. p values were obtained by ordinary one-way ANOVA.

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